Improvement of downstream processing of recombinant proteins by means of genetic engineering

Flaschel E, Friehs K (1993)
Biotechnology Advances 11(1): 31-77.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
OA
DOI
URN
urn:nbn:de:0070-pub-16461730
Autor*in
Flaschel, ErwinUniBi; Friehs, KarlUniBi
Einrichtung
Technische Fakultät
Abstract / Bemerkung
The rapid advancement of genetic engineering has allowed to produce an impressive number of proteins on a scale which would not have been achieved by classical biotechnology. At the beginning of this development research was focussed on elucidating the mechanisms of protein overexpression. The appearance of inclusion bodies may illustrate the success. In the meantime, genetic engineering is not only expected to achieve overexpression, but to improve the whole process of protein production. For downstream processing of recombinant proteins, the synthesis of fusion proteins is of primary importance. Fusion with certain proteins or peptides may protect the target protein from proteolytic degradation and may alter its solubility. Intracellular proteins may be translocated by means of fusions with signal peptides. Affinity tags as fusion complements may render protein separation and purification highly selective. These methods as well as similar ones for improving the downstream processing of proteins will be discussed on the basis of recent literature.
Stichworte
GENETIC ENGINEERING; DOWNSTREAM PROCESSING; PROTEIN EXPORT; SECRETION; PROTEIN; AFFINITY HANDLE; PURIFICATION TAG; FUSION COMPLEMENT; PROTEIN; FUSION; RECOMBINANT PROTEIN
Erscheinungsjahr
1993
Zeitschriftentitel
Biotechnology Advances
Band
11
Ausgabe
1
Seite(n)
31-77
ISSN
0734-9750
Page URI
https://pub.uni-bielefeld.de/record/1646173

Zitieren

Flaschel E, Friehs K. Improvement of downstream processing of recombinant proteins by means of genetic engineering. Biotechnology Advances. 1993;11(1):31-77.
Flaschel, E., & Friehs, K. (1993). Improvement of downstream processing of recombinant proteins by means of genetic engineering. Biotechnology Advances, 11(1), 31-77. https://doi.org/10.1016/0734-9750(93)90409-G
Flaschel, Erwin, and Friehs, Karl. 1993. “Improvement of downstream processing of recombinant proteins by means of genetic engineering”. Biotechnology Advances 11 (1): 31-77.
Flaschel, E., and Friehs, K. (1993). Improvement of downstream processing of recombinant proteins by means of genetic engineering. Biotechnology Advances 11, 31-77.
Flaschel, E., & Friehs, K., 1993. Improvement of downstream processing of recombinant proteins by means of genetic engineering. Biotechnology Advances, 11(1), p 31-77.
E. Flaschel and K. Friehs, “Improvement of downstream processing of recombinant proteins by means of genetic engineering”, Biotechnology Advances, vol. 11, 1993, pp. 31-77.
Flaschel, E., Friehs, K.: Improvement of downstream processing of recombinant proteins by means of genetic engineering. Biotechnology Advances. 11, 31-77 (1993).
Flaschel, Erwin, and Friehs, Karl. “Improvement of downstream processing of recombinant proteins by means of genetic engineering”. Biotechnology Advances 11.1 (1993): 31-77.
Alle Dateien verfügbar unter der/den folgenden Lizenz(en):
Copyright Statement:
Dieses Objekt ist durch das Urheberrecht und/oder verwandte Schutzrechte geschützt. [...]
Volltext(e)
Name
Access Level
OA Open Access
Zuletzt Hochgeladen
2019-09-06T08:48:06Z
MD5 Prüfsumme
3034aa1a828fd647e589e88946a33aca


11 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

A bio-basis function neural network for protein peptide cleavage activity characterisation.
Yang ZR, Dry J, Thomson R, Charles Hodgman T., Neural Netw 19(4), 2006
PMID: 16478661
How to find soluble proteins: a comprehensive analysis of alpha/beta hydrolases for recombinant expression in E. coli.
Koschorreck M, Fischer M, Barth S, Pleiss J., BMC Genomics 6(), 2005
PMID: 15804363
Current and prospective applications of metal ion-protein binding.
Ueda EK, Gout PW, Morganti L., J Chromatogr A 988(1), 2003
PMID: 12647817
Searching for discrimination rules in protease proteolytic cleavage activity using genetic programming with a min-max scoring function.
Yang ZR, Thomson R, Hodgman TC, Dry J, Doyle AK, Narayanan A, Wu X., Biosystems 72(1-2), 2003
PMID: 14642665
Host selection as a downstream strategy: polyelectrolyte precipitation of beta-glucuronidase from plant extracts.
Menkhaus TJ, Eriksson SU, Whitson PB, Glatz CE., Biotechnol Bioeng 77(2), 2002
PMID: 11753921
Applications of novel affinity cassette methods: use of peptide fusion handles for the purification of recombinant proteins.
Hearn MT, Acosta D., J Mol Recognit 14(6), 2001
PMID: 11757069
Facilitated downstream processing of a histidine-tagged protein from unclarified E. coli homogenates using immobilized metal affinity expanded-bed adsorption.
Clemmitt RH, Chase HA., Biotechnol Bioeng 67(2), 2000
PMID: 10592518
Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins.
Nilsson J, Ståhl S, Lundeberg J, Uhlén M, Nygren PA., Protein Expr Purif 11(1), 1997
PMID: 9325133
The green fluorescent protein is a versatile reporter for bioprocess monitoring.
Poppenborg L, Friehs K, Flaschel E., J Biotechnol 58(2), 1997
PMID: 9383982
A fusion protein designed for noncovalent immobilization: stability, enzymatic activity, and use in an enzyme reactor.
Stempfer G, Höll-Neugebauer B, Kopetzki E, Rudolph R., Nat Biotechnol 14(4), 1996
PMID: 9630924
Improving protein extraction yield in reversed micellar systems through surface charge engineering.
Pires MJ, Martel P, Baptista A, Petersen SB, Willson RC, Cabral JM., Biotechnol Bioeng 44(7), 1994
PMID: 18618844

286 References

Daten bereitgestellt von Europe PubMed Central.

Towards the Chemical Synthesis of Proteins
Bayer, Angew. Chem. - Int. Ed. 30(2), 1991
Physikalisch-chemische Trennverfahren in der Biotechnologie
Onken, Chem.-Ing.-Tech. 61(5), 1989
Biotechnology: status and perspectives
Wang, AIChE Monograph Ser. 84(18), 1988
Downstream processing of proteins: recent advances.
Ogez JR, Hodgdon JC, Beal MP, Builder SE., Biotechnol. Adv. 7(4), 1989
PMID: 14542986
An overview of continuous protein purification processes.
Gordon NF, Moore CM, Cooney CL., Biotechnol. Adv. 8(4), 1990
PMID: 14543694
The Primary Stages of Protein Recovery
Lee, J. Biotechnol. 11(), 1989
High-Resolution Fractionation of Proteins in Downstream Processing
Hammond, J. Biotechnol. 11(), 1989

AUTHOR UNKNOWN, 1989

AUTHOR UNKNOWN, 1989

AUTHOR UNKNOWN, 1989

AUTHOR UNKNOWN, 1987

AUTHOR UNKNOWN, 1990

AUTHOR UNKNOWN, 1990

AUTHOR UNKNOWN, 1990

AUTHOR UNKNOWN, 1989
Engineering proteins for purification.
Sassenfeld HM., Trends Biotechnol. 8(4), 1990
PMID: 1366529
Manufacturing New-Generation Proteins: Part I + II
Hammond, Pharm. Tech. Int. (), 1991
Manufacturing New-Generation Proteins: Part I + II
Hammond, Pharm. Tech. Int. (), 1991
Gene fusions for purpose of expression: an introduction.
Uhlen M, Moks T., Meth. Enzymol. 185(), 1990
PMID: 2199775
Protein fusions: bioseparation and application.
Sherwood R., Trends Biotechnol. 9(1), 1991
PMID: 1366921
The Kinetics of Plasmid Loss
Summers, Trends Biotechnol. 9(8), 1991
Strategies for improving plasmid stability in genetically modified bacteria in bioreactors.
Kumar PK, Maschke HE, Friehs K, Schugerl K., Trends Biotechnol. 9(8), 1991
PMID: 1367568
Runaway-replication plasmids as tools to produce large quantities of proteins from cloned genes in bacteria.
Nordstrom K, Uhlin BE., Biotechnology (N.Y.) 10(6), 1992
PMID: 1368887
High level heterologous expression in E. coli using mutant forms of the lac promoter.
Makoff AJ, Oxer MD., Nucleic Acids Res. 19(9), 1991
PMID: 2041779
A new system for the expression of human interleukin-6 in Escherichia coli
Yasukawa, Biotech. Lett. 12(), 1990
Modified bacteriophage lambda promoter vectors for overproduction of proteins in Escherichia coli.
Elvin CM, Thompson PR, Argall ME, Hendry P, Stamford NP, Lilley PE, Dixon NE., Gene 87(1), 1990
PMID: 2139621
Study of Vitreoscilla globin (vgb) gene expression and promoter activity in E. coli through transcriptional fusion.
Dikshit KL, Dikshit RP, Webster DA., Nucleic Acids Res. 18(14), 1990
PMID: 2198533

Pharmacia, Molecular and Cell Biology Cataloque (), 1991
Mechanisms of mRNA decay.
Brawerman G., Trends Biotechnol. 8(7), 1990
PMID: 1366620
Protein overproduction in Escherichia coli: RNA stabilization, cell disruption and recovery with a cross-flow microfiltration membrane.
Chan WK, Belfort M, Belfort G., J. Biotechnol. 18(3), 1991
PMID: 1370041
High level expression of Acinetobacter calcoaceticus mutarotase in Escherichia coli is achieved by improving the translational control sequence and removal of the signal sequence
Schmucker, Appl. Microb. Biotechnol. 30(), 1989
Enhancement of heterologous polypeptide expression by alterations in the ribosome-binding-site sequence
Olsen, J. Biotechnol. 9(), 1989
Optimizing the promoter and ribosome binding sequence for expression of human single chain urokinase-like plasminogen activator in Escherichia coli and stabilization of the product by avoiding heat shock response.
Surek B, Wilhelm M, Hillen W., Appl. Microbiol. Biotechnol. 34(4), 1991
PMID: 1367523
Expression of the rat interferon-alpha 1 gene in Escherichia coli controlled by the secondary structure of the translation-initiation region.
Spanjaard RA, van Dijk MC, Turion AJ, van Duin J., Gene 80(2), 1989
PMID: 2511076
Codon usage and gene expression
Ernst, Trends Biotechnol 6(), 1988
Minimizing proteolysis in Escherichia coli: genetic solutions.
Gottesman S., Meth. Enzymol. 185(), 1990
PMID: 2199774
Genetics of proteolysis in Escherichia coli*.
Gottesman S., Annu. Rev. Genet. 23(), 1989
PMID: 2694929
Unusual observation during construction of a new cloning vector providing lon gene expression in Escherichia coli
Friehs, J. Biotechnol. 9(), 1989
Fine-structure mapping and identification of two regulators of capsule synthesis in Escherichia coli K-12.
Brill JA, Quinlan-Walshe C, Gottesman S., J. Bacteriol. 170(6), 1988
PMID: 2836365
Intracellular expression of BPTI fusion proteins and single column cleavage/affinity purification by chymotrypsin.
Altman JD, Henner D, Nilsson B, Anderson S, Kuntz ID., Protein Eng. 4(5), 1991
PMID: 1716367
Conversion of a mitochondrial gene for mammalian cytochrome c oxidase subunit II into its universal codon equivalent and expression in vivo and in vitro.
Cao JL, Revzin A, Ferguson-Miller S., Biochemistry 30(10), 1991
PMID: 1848093
Effect of protein fusion on the stability of proteolytically sensitive sites in recombinant DNA proteins
Hellebust, J. Biotechnol. 12(), 1989
A Dual-Affinity Gene Fusion System to Express Small Recombinant Proteins in a Soluble Form: Expression and Characterization of Protein A Deletion Mutants
Jansson, Prot. Eng. 2(6), 1989
Dual Affinity Fusion Approach and Its Use to Express Recombinant Human Insulin-Like Growth Factor II
Hammarberg, 1989
Optimization of growth conditions for the production of proteolytically-sensitive proteins in the periplasmic space of Escherichia coli.
Baneyx F, Ayling A, Palumbo T, Thomas D, Georgiou G., Appl. Microbiol. Biotechnol. 36(1), 1991
PMID: 1367774
Purification of recombinant proteins for pharmaceutical use.
Farrell DJ., Biochem. Soc. Trans. 18(2), 1990
PMID: 2199262
Recombinant Proteins: Virtual Authenticity
Bialy, Bio/Technology 5(), 1987
The functional expression of antibody Fv fragments in Escherichia coli: improved vectors and a generally applicable purification technique.
Skerra A, Pfitzinger I, Pluckthun A., Biotechnology (N.Y.) 9(3), 1991
PMID: 1367302
Predicting the solubility of recombinant proteins in Escherichia coli.
Wilkinson DL, Harrison RG., Biotechnology (N.Y.) 9(5), 1991
PMID: 1367308
Protein Inclusion Body Formation and Purification
Krueger, BioPharm 2(), 1989
Crossflow Filtration for the Separation of Inclusion Bodies from Soluble Proteins in Recombinant Escherichia coli Cell lysate
Forman, J. Membrane Sci. 48(), 1990
Recovery of therapeutic proteins from inclusion bodies: problems and process strategies.
Thatcher DR., Biochem. Soc. Trans. 18(2), 1990
PMID: 2165931
Solubility as a function of protein structure and solvent components.
Schein CH., Biotechnology (N.Y.) 8(4), 1990
PMID: 1369261
Factors Influencing Inclusion Body Formation in the Production of a Fused Protein in Escherichia coli
Strandberg, Appl. Env. Microb. 57(), 1991
Cloning and overexpression of Moloney murine leukemia virus reverse transcriptase in Escherichia coli.
Kotewicz ML, D'Alessio JM, Driftmier KM, Blodgett KP, Gerard GF., Gene 35(3), 1985
PMID: 2412939
Integrated Process Design for Producing and Recovering Proteins from Inclusion Bodies
Titchener-Hooker, Pharm. Tech. Int. (), 1990
The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.
Fischer G, Schmid FX., Biochemistry 29(9), 1990
PMID: 2186809
Dominant forces in protein folding.
Dill KA., Biochemistry 29(31), 1990
PMID: 2207096
Folding and association of proteins.
Jaenicke R., Prog. Biophys. Mol. Biol. 49(2-3), 1987
PMID: 3327098
Downstream processing: key to slashing production costs 100 fold.
Spalding BJ., Biotechnology (N.Y.) 9(3), 1991
PMID: 1367296
Polyethylene glycol enhanced protein refolding.
Cleland JL, Builder SE, Swartz JR, Winkler M, Chang JY, Wang DI., Biotechnology (N.Y.) 10(9), 1992
PMID: 1368998
Chaperonin assisted polypeptide folding and assembly: implications for the production of functional proteins in bacteria.
Gatenby AA, Viitanen PV, Lorimer GH., Trends Biotechnol. 8(12), 1990
PMID: 1369447
Protein-catalysed protein folding.
Horwich AL, Neupert W, Hartl FU., Trends Biotechnol. 8(5), 1990
PMID: 1369433
Side-Specific Proteolysis of Fusion Proteins
Carter, 1990
Expression of human insulin-like growth factor I in bacteria: use of optimized gene fusion vectors to facilitate protein purification.
Moks T, Abrahmsen L, Holmgren E, Bilich M, Olsson A, Uhlen M, Pohl G, Sterky C, Hultberg H, Josephson S., Biochemistry 26(17), 1987
PMID: 3676250
A general method for retrieving the components of a genetically engineered fusion protein.
Szoka PR, Schreiber AB, Chan H, Murthy J., DNA 5(1), 1986
PMID: 3007060
Protein engineering of antibody binding sites: Recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli
Huston, 1988
Overexpression in Escherichia coli of a methionine-free designed interleukin-2 receptor (Tac protein) based on a chemically cleavable fusion protein.
Husken D, Beckers T, Engels JW., Eur. J. Biochem. 193(2), 1990
PMID: 2121481
The isolation and characterisation of human atrial natriuretic factor produced as a fusion protein in Escherichia coli.
Knott JA, Sullivan CA, Weston A., Eur. J. Biochem. 174(2), 1988
PMID: 2968245
Expression in Escherichia coli and characterization of human growth-hormone-releasing factor.
Villa S, De Fazio G, Donini S, Tarchi G, Canosi U., Eur. J. Biochem. 171(1-2), 1988
PMID: 3123227
Selective chemical cleavage of tryptophanyl peptide bonds by oxidative chlorination with N-chlorosuccinimide.
Shechter Y, Patchornik A, Burstein Y., Biochemistry 15(23), 1976
PMID: 990266
Genetic Approach to Facilitate Purification of Recombinant Proteins with a Novel Metal Chelate Adsorbent
Hochuli, Bio/Technology 11(), 1988
Chemical synthesis and cloning of a poly(arginine)-coding gene fragment designed to aid polypeptide purification.
Smith JC, Derbyshire RB, Cook E, Dunthorne L, Viney J, Brewer SJ, Sassenfeld HM, Bell LD., Gene 32(3), 1984
PMID: 6335699
High level expression in Escherichia coli of the DNA-binding domain of the glucocorticoid receptor in a functional form utilizing domain-specific cleavage of a fusion protein.
Dahlman K, Stromstedt PE, Rae C, Jornvall H, Flock JI, Carlstedt-Duke J, Gustafsson JA., J. Biol. Chem. 264(2), 1989
PMID: 2642905
Production of a site specifically cleavable P-glycoprotein-beta-galactosidase fusion protein.
Shimabuku AM, Saeki T, Ueda K, Komano T., Agric. Biol. Chem. 55(4), 1991
PMID: 1369454
A Novel Enzymatic Method for Production of Authentic hGH from an Escherichia coli Produced hGH-Precurser
Dalb∅ge, Bio/Technology 5(2), 1987
Production of epidermal growth factor in Escherichia coli from a synthetic gene.
Allen G, Paynter CA, Winther MD., J. Cell Sci. Suppl. 3(), 1985
PMID: 3938982
A Calcium-Dependent Antibody for Identification and Purification of Recombinant Proteins
Prickett, Bio Techniques 7(), 1989
Hydrophilic gels as immobilization materials and stabilizers for enzyme-catalysed esterification in organic media.
Hertzberg S, Fuskevag OM, Anthonsen T., Progress in biotechnology. 8(), 1992
PMID: IND93054912
Expression of an autoprocessing CAT-HIV-1 proteinase fusion protein: purification to homogeneity of the release 99 residue proteinase.
Montgomery DS, Singh OM, Gray NM, Dykes CW, Weir MP, Hobden AN., Biochem. Biophys. Res. Commun. 175(3), 1991
PMID: 2025253
Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli.
Louis JM, McDonald RA, Nashed NT, Wondrak EM, Jerina DM, Oroszlan S, Mora PT., Eur. J. Biochem. 199(2), 1991
PMID: 2070793
High-level expression of human BSF-2/IL-6 cDNA in Escherichia coli using a new type of expression-preparation system.
Tonouchi N, Oouchi N, Kashima N, Kawai M, Nagase K, Okano A, Matsui H, Yamada K, Hirano T, Kishimoto T., J. Biochem. 104(1), 1988
PMID: 2851586
Secretion of Human Superoxide Dismutase in Escherichia coli
Takahara, Bio/Technology 6(), 1988
Metal Affinity Chromatography of Recombinant HIV-1 Reverse Transcriptase Containing a Human Renin Cleavable Metal Binding Domain
Sharma, Biotech. Appl. Biochem. 14(), 1991
Engineering subtilisin BPN' for site-specific proteolysis.
Carter P, Nilsson B, Burnier JP, Burdick D, Wells JA., Proteins 6(3), 1989
PMID: 2516317
New vectors for high level expression of recombinant proteins in bacteria.
Hakes DJ, Dixon JE., Anal. Biochem. 202(2), 1992
PMID: 1519755
Cytotoxicity of a recombinant ricin-A-chain fusion protein containing a proteolytically-cleavable spacer sequence.
O'Hare M, Brown AN, Hussain K, Gebhardt A, Watson G, Roberts LM, Vitetta ES, Thorpe PE, Lord JM., FEBS Lett. 273(1-2), 1990
PMID: 2121540
Cloning and expression of a yeast ubiquitin-protein cleaving activity in Escherichia coli
Miller, Bio/Technology 7(), 1989
Genetic control of flocculation in Escherichia coli.
Ogden KL, Taylor AL., J. Ind. Microbiol. 7(4), 1991
PMID: 1369457
Bacterial cell disruption: a key unit operation in the recovery of intracellular products.
Harrison ST., Biotechnol. Adv. 9(2), 1991
PMID: 14548738
Large-scale protein extraction and isolation.
Scawen MD, Hammond PM, Sherwood RF, Atkinson T., Biochem. Soc. Trans. 18(2), 1990
PMID: 2379694
Purification of Proteins and the Disruption of Microbial Cells
Kula, Biotechnol. Progr. 3(), 1987
Intracellular Lytic Enzyme systems and their use for disruption of Escherichia coli
Dabora, Adv. Biochem. Eng. /Biotechnol. 43(), 1990

AUTHOR UNKNOWN, 0
Release of β-galactosidase from E. coli by a plasmid containing a temperature sensitive lytic function
Dabora, Biotech. Lett. 11(), 1989
Current status of secretion of foreign proteins by microorganisms
Nicaud, J. Biotechnol. 3(), 1986
Escherichia coli und die Biotechnologie - ein ideales Paar
Rasched, Chem. Lab. Biotech. 41(), 1990
Secretion and folding of human growth hormone in Escherichia coli.
Hsiung HM, Becker GW., Biotechnol. Genet. Eng. Rev. 6(), 1988
PMID: 3071375
Genetic studies on the inability of beta-galactosidase to be translocated across the Escherichia coli cytoplasmic membrane.
Lee C, Li P, Inouye H, Brickman ER, Beckwith J., J. Bacteriol. 171(9), 1989
PMID: 2527843
Continuous culture of Escherichia coli for extracellular production of recombinant amylase
Alexander, Biotechnol. Lett. 11(), 1989
Expression of a Escherichia coli preproinsulin fusion protein in Escherichia coli
Emerick, Bio/Technology 2(), 1984
Secretion and processing of an immunoglobulin light chain in Escherichia coli.
Zemel-Dreasen O, Zamir A., Gene 27(3), 1984
PMID: 6428978
Release of periplasmic enzymes and other physiological effects of beta-lactamase overproduction in Escherichia coli.
Georgiou G, Shuler ML, Wilson DB., Biotechnol. Bioeng. 32(6), 1988
PMID: 18587779
Production of rat epidermal growth factor by Escherichia coli cells containing a secretion plasmid
Ohgai, J. Biotechnol. 10(), 1989
Illicit secretion of a cytoplasmic protein into the periplasm of Escherichia coli requires a signal peptide plus a portion of the cognate secreted protein. Demarcation of the critical region of the mature protein.
Summers RG, Knowles JR., J. Biol. Chem. 264(33), 1989
PMID: 2684968
Export and purification of a cytoplasmic dimeric protein by fusion to the maltose-binding protein of Escherichia coli.
Blondel A, Bedouelle H., Eur. J. Biochem. 193(2), 1990
PMID: 2226455
Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space.
Bedouelle H, Duplay P., Eur. J. Biochem. 171(3), 1988
PMID: 3278900
Expression and purification of native human granulocyte-macrophage colony-stimulating factor from an Escherichia coli secretion vector.
Libby RT, Braedt G, Kronheim SR, March CJ, Urdal DL, Chiaverotti TA, Tushinski RJ, Mochizuki DY, Hopp TP, Cosman D., DNA 6(3), 1987
PMID: 3297585
Secretion of mature human interferon alpha 2 into the periplasmic space of Escherichia coli
Barbero, J. Biotechnol. 4(), 1986
Expression and secretion of Mirabilis antiviral protein in Escherichia coli and its inhibition of in vitro eukaryotic and prokaryotic protein synthesis.
Habuka N, Akiyama K, Tsuge H, Miyano M, Matsumoto T, Noma M., J. Biol. Chem. 265(19), 1990
PMID: 2193030
Expression of the chemically synthesized coding region for the cytotoxin alpha-sarcin in Escherichia coli using a secretion cloning vector.
Henze PP, Hahn U, Erdmann VA, Ulbrich N., Eur. J. Biochem. 192(1), 1990
PMID: 2205498
Periplasmic production of human pancreatic prokallikrein in Escherichia coli
Shibui, Appl. Microb. Biotechnol. 31(), 1989
Production of native, correctly folded bovine pancreatic trypsin inhibitor by Escherichia coli.
Marks CB, Vasser M, Ng P, Henzel W, Anderson S., J. Biol. Chem. 261(16), 1986
PMID: 2423515
Efficacies of Different Secretion Vectors for Secretion of Human Epidermal Growth Factor by Escherichia coli
Oka, Agric. Biol. Chem. 51(4), 1987
Expression of chemically synthesized alpha-neo-endorphin gene fused to E. coli alkaline phosphatase.
Ohsuye K, Nomura M, Tanaka S, Kubota I, Nakazato H, Shinagawa H, Nakata A, Noguchi T., Nucleic Acids Res. 11(5), 1983
PMID: 6298740
Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein.
di Guan C, Li P, Riggs PD, Inouye H., Gene 67(1), 1988
PMID: 2843437
Secretion of recombinant ribonuclease T1 into the periplasmic space of Escherichia coli with the aid of the signal peptide of alkaline phosphatase.
Fujimura T, Tanaka T, Ohara K, Morioka H, Uesugi S, Ikehara M, Nishikawa S., FEBS Lett. 265(1-2), 1990
PMID: 2114313
Expression vector promoting the synthesis and export of the human growth-hormone-releasing factor in Escherichia coli.
Anba J, Baty D, Lloubes R, Pages JM, Joseph-Liauzun E, Shire D, Roskam W, Lazdunski C., Gene 53(2-3), 1987
PMID: 3301532
Expression and characterization of a recombinant human parathyroid hormone secreted by Escherichia coli employing the staphylococcal protein A promoter and signal sequence.
Hogset A, Blingsmo OR, Saether O, Gautvik VT, Holmgren E, Hartmanis M, Josephson S, Gabrielsen OS, Gordeladze JO, Alestrom P., J. Biol. Chem. 265(13), 1990
PMID: 2185244
Purification and Characterization of Recombinant Human Insulin-Like Growth Factor II (IGF-II) Expressed as a Secreted Fusion Protein in Escherichia coli
Wadenstein, Biotech. Appl. Biochem. 13(3), 1991
Chicken ovalbumin is synthesized and secreted by Escherichia coli
Fraser, 1978
The normally periplasmic enzyme beta-lactamase is specifically and efficiently translocated through the Escherichia coli outer membrane when it is fused to the cell-surface enzyme pullulanase.
Kornacker MG, Pugsley AP., Mol. Microbiol. 4(7), 1990
PMID: 2233249
An 'internal' signal sequence directs secretion and processing or proinsulin in bacteria.
Talmadge K, Brosius J, Gilbert W., Nature 294(5837), 1981
PMID: 7029306
Modified enterotoxin signal sequences increase secretion level of the recombinant human epidermal growth factor in Escherichia coli.
Morioka-Fujimoto K, Marumoto R, Fukuda T., J. Biol. Chem. 266(3), 1991
PMID: 1988446

AUTHOR UNKNOWN, 0
Cloning and expression in Escherichia coli of the Serratia marcescens metalloprotease gene: secretion of the protease from E. coli in the presence of the Erwinia chrysanthemi protease secretion functions.
Letoffe S, Delepelaire P, Wandersman C., J. Bacteriol. 173(7), 1991
PMID: 2007544
Engineering Protein Export in Escherichia coli: The Cloacine DF13 System
van, 1987
Secretion of haemolysin by Escherichia coli.
Mackman N, Nicaud JM, Gray L, Holland IB., Curr. Top. Microbiol. Immunol. 125(), 1986
PMID: 3017638
Use of alkaline phosphatase fusions to study protein secretion in Bacillus subtilis.
Payne MS, Jackson EN., J. Bacteriol. 173(7), 1991
PMID: 1901054
Production of heterologous proteins in Bacillus subtilis: the effect of the joint between signal sequence and mature protein on yield.
Hemila H, Sibakov M., Appl. Microbiol. Biotechnol. 36(1), 1991
PMID: 1367777
Secretion of human growth hormone in Bacillus subtilis using prepropeptide coding region of Bacillus amyloliquefaciens neutral protease gene
Honjo, J. Biotechnol. 4(), 1986
Expression of human papillomavirus proteins in yeast Saccharomyces cerevisiae.
Carter JJ, Yaegashi N, Jenison SA, Galloway DA., Virology 182(2), 1991
PMID: 1850917
Purification of extracellular alkaline phosphatase released by Escherichia coli excretory mutants
Atlan, Appl. Microbiol. Biotechnol. 26(), 1987
Synthèse et excrétion de β-lactamase chez une souche sauvage non excrétrice et un mutant excréteur d'Escherichia coli K-12
Fognini-Lefebvre, C.R. Acad. Sc. Paris t. 296(), 1983
Formation of proinsulin by immobilized Bacillus subtilis.
Mosbach K, Birnbaum S, Hardy K, Davies J, Bulow L., Nature 302(5908), 1983
PMID: 6403870
Escherichia coli strains with defined mutations which alter cellular permeability
Sampson, J. Ind. Microb. 1(), 1987
Erythropoietin-beta-D-galactosidase. The generation, purification and use of a fusion protein.
Nielsen OJ, Costa-Giomi P, Weinmann R, Erslev AJ, Caro J., J. Immunol. Methods 111(1), 1988
PMID: 3134487
The construction and characterization of a biologically active recombinant IL-2 containing a lysine-rich C-terminal extension.
Lin Y, Robb RJ, Gray JE, Simon P., J. Immunol. 141(11), 1988
PMID: 3263437
New developments in downstream processing
Lowe, J. Biotechnol. 1(), 1984
Affinity chromatography supports: a look at performance requirements.
Narayanan SR, Crane LJ., Trends Biotechnol. 8(1), 1990
PMID: 1369265
Antibody engineering: advances from the use of Escherichia coli expression systems.
Pluckthun A., Biotechnology (N.Y.) 9(6), 1991
PMID: 1367224

AUTHOR UNKNOWN, 1989
Fusions to staphylococcal protein A.
Nilsson B, Abrahmsen L., Meth. Enzymol. 185(), 1990
PMID: 2199777
Directed Molecular Evolution
Joice, Sci. Amer. 267(6), 1992
Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase.
Tuerk C, Gold L., Science 249(4968), 1990
PMID: 2200121
Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions.
Porath J, Olin B., Biochemistry 22(7), 1983
PMID: 6849872

AUTHOR UNKNOWN, 0
New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues.
Hochuli E, Dobeli H, Schacher A., J. Chromatogr. 411(), 1987
PMID: 3443622
High-Performance Metal Chelate Interaction Chromatography of Proteins with Silica-Bound Ethylene Diamine-N,N'-Diacetic Acid,
Bacolod, J. Chromatogr. 512(), 1990
Purification of Proteins by IMAC
Sulkowski, Trends Biotechnol. 3(1), 1985
Protein interactions with immobilized transition metal ions: quantitative evaluations of variations in affinity and binding capacity.
Hutchens TW, Yip TT., Anal. Biochem. 191(1), 1990
PMID: 2077938
Large-scale chromatography of recombinant proteins.
Hochuli E., J. Chromatogr. 444(), 1988
PMID: 3060478
Protein Purification
Lillehoj, Adv. Biochem. Eng./Biotechnol. 40(), 1989
Large scale protein separations: engineering aspects of chromatography.
Chisti Y, Moo-Young M., Biotechnol. Adv. 8(4), 1990
PMID: 14543691
Enzyme Purification by Affinity Chromatography Combined with Batchwise Adsorption and Columnwise Elution
Yang, J. Chem. Eng. Japan 22(5), 1989
Isolation and Purification of Endo-Polygalactoronase by Affinity Chromatography in a Fluidized Bed Reactor
Somers, Chem. Eng. J. 40(), 1989
Bioproduct Recovery from Unclaryfied Broth and Homogenates Using Immobilized Adsorbents
Nigam, Biotech. Progr. 4(3), 1988

AUTHOR UNKNOWN, 0

AUTHOR UNKNOWN, 0
Simultaneous ultrafiltration and affinity sorptive separation of proteins in a hollow fiber membrane module.
Molinari R, Torres JL, Michaels AS, Kilpatrick PK, Carbonell RG., Biotechnol. Bioeng. 36(6), 1990
PMID: 18595115
Proteinreinigung durch Affinitätsverfahren und Membranen
Aigner, BioTec 2(2), 1991
Proteinchromatographie mit modifizierten Membranen
Briefs, 1991

AUTHOR UNKNOWN, Biosep. 1(3–4), 1990
Preparation of Technical Grade Polyethylene Glycol (PEG) (MTr 20000)-N-(2-Aminoethyl)-NADH by a Procedure Adaptable to Large-Scale Synthesis
Bückmann, Biotech. Appl. Biochem. 9(), 1987
Aqueous two-phase metal affinity extraction of heme proteins.
Wuenschell GE, Naranjo E, Arnold FH., Bioprocess engineering. 5(5), 1990
PMID: IND90053464
Reactive (Affinity) Extraction of Enzymes from Biomass
Schustolla, Ber. Bunsenges. Phys. Chem. 93(), 1989
Novel Affinity-Based Processes for Protein Purification
Chen, J. Ferment. Bioeng. 70(3), 1990
Affinity partition between aqueous phases - a tool for large-scale purification of enzymes
Johansson, J. Biotechnol. 11(), 1989
Affinity extraction of proteins from biomass - metal affinity extraction of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei
Schustolla, 1990
Bioaffinity separations using reversed micellar extraction
Woll, Biotech. Progr. 5(2), 1989
Metal Affinity Precipitation of Proteins
van, Biotech. Appl. Biochem. 11(), 1989
Affinity precipitation of extracellular microbial enzymes
Pécs, J. Biotechnol. 21(), 1991
Ultrafiltration for the Separation of Biocatalysts
Flaschel, Adv. Biochem. Eng./Biotechnol. 26(), 1983
The Prospects for Large-Scale Electrophoreses
Ivory, Sep. Sci. Technol. 23(8–9), 1988
Continuous Separation of Proteins by Free-Flow Zone Electrophoresis
Nath, Ber. Bunsenges. Phys. Chem. 93(), 1989
Free Flow Electrophoresis as a Purification Step of High Versatility for Bioproducts
Rutte, Ber. Bunsenges. Phys. Chem. 93(), 1989

Righetti, 1990

Medac, 1991

International, The FLAG Biosystem (), 1991

Moks, Bio/Technology 5(), 1987

Diagen, The QIAexpressionist (), 1991
Partitioning of beta-galactosidase fusion proteins in PEG/potassium phosphate aqueous two-phase systems.
Kohler K, Veide A, Enfors SO., Enzyme Microb. Technol. 13(3), 1991
PMID: 1367498
Extraction of β-galactosidase fused protein A in aqueous two-phase systems
Veide, Enzyme Microb. Technol. 9(), 1987
Engineering proteins to enhance their partition coefficients in aqueous two-phase systems.
Kohler K, Ljungquist C, Kondo A, Veide A, Nilsson B., Biotechnology (N.Y.) 9(7), 1991
PMID: 1367659
Characterization of His-X3-His sites in alpha-helices of synthetic metal-binding bovine somatotropin.
Suh SS, Haymore BL, Arnold FH., Protein Eng. 4(3), 1991
PMID: 1713327
Recovery of a charged-fusion protein from cell extracts by polyelectrolyte precipitation.
Parker DE, Glatz CE, Ford CF, Gendel SM, Suominen I, Rougvie MA., Biotechnol. Bioeng. 36(5), 1990
PMID: 18595103
Polyelectrolyte precipitation of beta-galactosidase fusions containing poly-aspartic acid tails.
Zhao JY, Ford CF, Glatz CE, Rougvie MA, Gendel SM., J. Biotechnol. 14(3-4), 1990
PMID: 1367483
Novel Metal-Affinity Protein Separations
Suh, 1990
Carbohydrate-recognition domains as tools for rapid purification of recombinant eukaryotic proteins.
Taylor ME, Drickamer K., Biochem. J. 274 ( Pt 2)(), 1991
PMID: 2006918
A Short Polypeptide Marker Sequence Useful for Recombinant Protein Identification and Purification.
Hopp TP, Prickett KS, Price VL, Libby RT, March CJ, Cerretti DP, Urdal DL, Conlon PJ., Biotechnology (N.Y.) 6(), 1988
PMID: c6853
Construction and properties of bifunctionally active membrane-bound fusion proteins. Escherichia coli proline carrier linked with beta-galactosidase.
Hanada K, Yamato I, Anraku Y., J. Biol. Chem. 262(29), 1987
PMID: 3115984
Purification and reconstitution of Escherichia coli proline carrier using a site specifically cleavable fusion protein.
Hanada K, Yamato I, Anraku Y., J. Biol. Chem. 263(15), 1988
PMID: 3130379
Overproduction and purification of the Tn10-specified inner membrane tetracycline resistance protein Tet using fusions to beta-galactosidase.
Hickman RK, McMurry LM, Levy SB., Mol. Microbiol. 4(8), 1990
PMID: 2177817
Immobilization and purification of enzymes with staphylococcal protein A gene fusion vectors.
Nilsson B, Abrahmsen L, Uhlen M., EMBO J. 4(4), 1985
PMID: 2990908
Efficient secretion and purification of human insulin-like growth factor I with a gene fusion vector in Staphylococci.
Nilsson B, Holmgren E, Josephson S, Gatenbeck S, Philipson L, Uhlen M., Nucleic Acids Res. 13(4), 1985
PMID: 3889837

AUTHOR UNKNOWN, 0
Affinity immobilization of a genetically engineered bifunctional hybrid protein.
Baneyx F, Schmidt C, Georgiou G., Enzyme Microb. Technol. 12(5), 1990
PMID: 1366486
Expression in Escherichia coli of the genes coding for reaction center subunits from Rhodobacter sphaeroides: wild-type proteins and fusion proteins containing one or four truncated domains from Staphylococcus aureus protein A at the carboxy-terminus.
Sohlemann P, Oeckl C, Michel H., Biochim. Biophys. Acta 1089(1), 1991
PMID: 2025640
One-step purification of hybrid proteins which have beta-galactosidase activity.
Ullmann A., Gene 29(1-2), 1984
PMID: 6436145
Rapid Purification of a Cloned Gene Product by Genetic Fusion and Side-Specific Proteolysis
Germino, 1984
A plasmid vector system for the expression of a triprotein consisting of beta-galactosidase, a collagenase recognition site and a foreign gene product.
Scholtissek S, Grosse F., Gene 62(1), 1988
PMID: 2836270
Autoflavinylation of Apo6-Hydroxy-D-Nicotin Oxydase
Brandsch, J. Biol. Chem. 266(28), 1991

AUTHOR UNKNOWN, 0
Expression of atrial natriuretic factor as a cleavable fusion protein with chloramphenicol acetyltransferase in Escherichia coli.
Dykes CW, Bookless AB, Coomber BA, Noble SA, Humber DC, Hobden AN., Eur. J. Biochem. 174(2), 1988
PMID: 2968246
Recombinant fusion proteins of protein A and protein G with glutathione S-transferase as reporter molecules.
Lew AM, Beck DJ, Thomas LM., J. Immunol. Methods 136(2), 1991
PMID: 1999651
Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase.
Smith DB, Johnson KS., Gene 67(1), 1988
PMID: 3047011
Xylanases from Streptomyces cyaneus.
Wang P, Ali S, Mason JC, Sims PFG, Broda P., Progress in biotechnology. 7(), 1991
PMID: IND93005184
Enzyme immobilization using the cellulose-binding domain of a cellulomonas fimi exoglucanase
Ong, Bio/Technology 7(), 1989
Enzyme immobilization using a cellulose-binding domain: properties of a beta-glucosidase fusion protein.
Ong E, Gilkes NR, Miller RC Jr, Warren AJ, Kilburn DG., Enzyme Microb. Technol. 13(1), 1991
PMID: 1367528
The Cellulose-Binding Domains of Cellulases: Tool for Biotechnology
Ong, Trends Biotechnol. 7(), 1989

AUTHOR UNKNOWN, 0
Analysis and use of the serum albumin binding domains of streptococcal protein G.
Nygren PA, Eliasson M, Abrahmsen L, Uhlen M, Palmcrantz E., J. Mol. Recognit. 1(2), 1988
PMID: 3273653
An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein.
Maina CV, Riggs PD, Grandea AG 3rd, Slatko BE, Moran LS, Tagliamonte JA, McReynolds LA, Guan CD., Gene 74(2), 1988
PMID: 3073105
Engineering the quaternary structure of an exported protein with a leucine zipper.
Blondel A, Bedouelle H., Protein Eng. 4(4), 1991
PMID: 1881871
Expression and Purification of the Leucine Zipper and DNA-Binding Domains of Fos and Jun: Both Fos and Jun Contact DNA Directly
Abate, 1990
Rapid purification of homodimer and heterodimer HIV-1 reverse transcriptase by metal chelate affinity chromatography.
Le Grice SF, Gruninger-Leitch F., Eur. J. Biochem. 187(2), 1990
PMID: 1688798
Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins.
Smith MC, Furman TC, Ingolia TD, Pidgeon C., J. Biol. Chem. 263(15), 1988
PMID: 3284883
Immobilization and affinity purification of recombinant proteins using histidine peptide fusions.
Ljungquist C, Breitholtz A, Brink-Nilsson H, Moks T, Uhlen M, Nilsson B., Eur. J. Biochem. 186(3), 1989
PMID: 2514094
The Purification of Recombinant Proteins Using C-Terminal Polyarginin Fusions
Brewer, Trends Biotechnol. 3(5), 1985
A Polypeptide Fusion Designed for the Purification of Recombinant Proteins
Sassenfeld, Bio/Technology 2(), 1984
Enzyme purification by genetically attached polycysteine and polyphenylalanine affinity tails.
Persson M, Bergstrand MG, Bulow L, Mosbach K., Anal. Biochem. 172(2), 1988
PMID: 3142291
Engineering enzyme specificity by "substrate-assisted catalysis".
Carter P, Wells JA., Science 237(4813), 1987
PMID: 3299704
Control of RNase E-mediated RNA degradation by 5'-terminal base pairing in E. coli.
Bouvet P, Belasco JG., Nature 360(6403), 1992
PMID: 1280335
Control of in vivo proteolysis in the production of recombinant proteins.
Enfors SO., Trends Biotechnol. 10(9), 1992
PMID: 1369412

AUTHOR UNKNOWN, 0
Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase.
Hartman J, Daram P, Frizzell RA, Rado T, Benos DJ, Sorscher EJ., Biotechnol. Bioeng. 39(8), 1992
PMID: 18601017
The folding of hen lysozyme involves partially structured intermediates and multiple pathways.
Radford SE, Dobson CM, Evans PA., Nature 358(6384), 1992
PMID: 1641003
Protein folding. Cytosolic chaperonin confirmed.
Ellis J., Nature 358(6383), 1992
PMID: 1352857
TCP1 complex is a molecular chaperone in tubulin biogenesis.
Yaffe MB, Farr GW, Miklos D, Horwich AL, Sternlicht ML, Sternlicht H., Nature 358(6383), 1992
PMID: 1630491
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol.
Lewis VA, Hynes GM, Zheng D, Saibil H, Willison K., Nature 358(6383), 1992
PMID: 1630492
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.
Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU., Nature 356(6371), 1992
PMID: 1349157
Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli.
Lee SC, Olins PO., J. Biol. Chem. 267(5), 1992
PMID: 1346610
Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation.
Sherman MYu , Goldberg AL., Nature 357(6374), 1992
PMID: 1349729
Renaturation of a single-chain immunotoxin facilitated by chaperones and protein disulfide isomerase.
Buchner J, Brinkmann U, Pastan I., Biotechnology (N.Y.) 10(6), 1992
PMID: 1369490
Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding
Schönbrunner, 1992
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.
Kamitani S, Akiyama Y, Ito K., EMBO J. 11(1), 1992
PMID: 1740115
An evaluation of different enzymatic cleavage methods for recombinant fusion proteins, applied on des(1-3)insulin-like growth factor I.
Forsberg G, Baastrup B, Rondahl H, Holmgren E, Pohl G, Hartmanis M, Lake M., J. Protein Chem. 11(2), 1992
PMID: 1388667
Production of recombinant human glucagon in the form of a fusion protein in Escherichia coli; recovery of glucagon by sequence-specific digestion.
Ishizaki J, Tamaki M, Shin M, Tsuzuki H, Yoshikawa K, Teraoka H, Yoshida N., Appl. Microbiol. Biotechnol. 36(4), 1992
PMID: 1368201
Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex.
Luirink J, High S, Wood H, Giner A, Tollervey D, Dobberstein B., Nature 359(6397), 1992
PMID: 1279430
The E. coli ffh gene is necessary for viability and efficient protein export.
Phillips GJ, Silhavy TJ., Nature 359(6397), 1992
PMID: 1331806
Bacillus subtilis and its relatives: molecular biological and industrial workhorses.
Harwood CR., Trends Biotechnol. 10(7), 1992
PMID: 1368322
Transfer and Expression of Heterologous Genes in Yeasts Other Than Saccharomyces cerevisiae
Reiser, Adv. Biochem. Eng./Biotechnol. 43(), 1990
Die methylotrophe Hefe Hansenula polymorpha als Expressionssystem für heterologe Proteine
Gellissen, BioEng. 5(), 1990
Kluyveromyces as a host for heterologous gene expression: expression and secretion of prochymosin.
van den Berg JA, van der Laken KJ, van Ooyen AJ, Renniers TC, Rietveld K, Schaap A, Brake AJ, Bishop RJ, Schultz K, Moyer D., Biotechnology (N.Y.) 8(2), 1990
PMID: 1366557
Genetics and Genetic Engineering of the Industrial Yeast Yarrowia lipolytica
Heslot, Adv. Biochem. Eng./Biotechnol. 43(), 1990
Transformation of different strains of Escherichia coli with multicopy plasmids carrying the phoA gene causes the secretion of periplasmic alkaline phosphatase and the accumulation of its precursor
Nesmeyanova, Mol. Biol. 25(3), 1991
Rites of passage: moving biotech proteins through the ER.
Edgington SM., Biotechnology (N.Y.) 10(11), 1992
PMID: 1369017
Processing by OmpT of fusion proteins carrying the HlyA transport signal during secretion by the Escherichia coli hemolysin transport system.
Hanke C, Hess J, Schumacher G, Goebel W., Mol. Gen. Genet. 233(1-2), 1992
PMID: 1603076
Processing of the prepropeptide portions of the Bacillus amyloliquefaciens neutral protease fused to Bacillus subtilis alpha-amylase and human growth hormone during secretion in Bacillus subtilis.
Nakayama A, Shimada H, Furutani Y, Honjo M., J. Biotechnol. 23(1), 1992
PMID: 1367948
Structure of yeast pGKL 128-kDa killer-toxin secretion signal sequence. Processing of the 128-kDa killer-toxin-secretion-signal-alpha-amylase fusion protein.
Tokunaga M, Kawamura A, Omori A, Hishinuma F., Eur. J. Biochem. 203(3), 1992
PMID: 1735428
Construction, bacterial expression and characterization of a bifunctional single-chain antibody-phosphatase fusion protein targeted to the human erbB-2 receptor.
Wels W, Harwerth IM, Zwickl M, Hardman N, Groner B, Hynes NE., Biotechnology (N.Y.) 10(10), 1992
PMID: 1369487

AUTHOR UNKNOWN, 0
Production of Recombinant Porcine Tumor Necrosis Factor Alpha in a Novel E. coli Expression System
Su, Bio/Technol. 13(5), 1992
A Modified Vector for the Controlled High-Level Overproduction of Staphylococcal Protein A Fusion Proteins in the Periplasm of Escherichia coli
Engel, Protein Expression Purification 3(), 1992
Fusions to the 5' end of a gene encoding a two-domain analogue of staphylococcal protein A.
Rondahl H, Nilsson B, Holmgren E., J. Biotechnol. 25(3), 1992
PMID: 1368804
Engineering metal binding sites into recombinant proteins for facile purification.
Smith MC., Ann. N. Y. Acad. Sci. 646(), 1991
PMID: 1809199

AUTHOR UNKNOWN, 0
Single-step purification on DEAE-sephacel of recombinant polypeptides produced in Escherichia coli.
Ortega S, Garcia JL, Zazo M, Varela J, Munoz-Willery I, Cuevas P, Gimenez-Gallego G., Biotechnology (N.Y.) 10(7), 1992
PMID: 1377476
Immobilization and single-step purification of fusion proteins using DEAE-cellulose.
Sanchez-Puelles JM, Sanz JM, Garcia JL, Garcia E., Eur. J. Biochem. 203(1-2), 1992
PMID: 1730220
A universal expression-purification system based on the coiled-coil interaction of myosin heavy chain.
Wolber V, Maeda K, Schumann R, Brandmeier B, Wiesmuller L, Wittinghofer A., Biotechnology (N.Y.) 10(8), 1992
PMID: 1368985
Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain.
Van Dyke MW, Sirito M, Sawadogo M., Gene 111(1), 1992
PMID: 1547959

AUTHOR UNKNOWN, 0
Molecular and cellular targeting in the expression of foreign polypeptides in bacteria.
Clement JM, Charbit A, Leclerc C, Martineau P, Muir S, O'Callaghan D, Popescu O, Szmelcman S, Hofnung M., Antonie Van Leeuwenhoek 61(2), 1992
PMID: 1580616
A plasmid expression vector that permits stabilization of both mRNAs and proteins encoded by the cloned genes.
Duvoisin RM, Belin D, Krisch HM., Gene 45(2), 1986
PMID: 3026907
Protein secretion in gram-positive bacteria.
Freudl R., J. Biotechnol. 23(3), 1992
PMID: 1368245
Decay of ompA mRNA and processing of 9S RNA are immediately affected by shifts in growth rate, but in opposite manners.
Georgellis D, Arvidson S, von Gabain A., J. Bacteriol. 174(16), 1992
PMID: 1644765
Enhanced production and recovery of recombinant proteins genetically targeted into the periplasm - E. coli penicillin acylase as an initial model system
Glisin, 1991
Human hemoglobin expression in Escherichia coli: importance of optimal codon usage.
Hernan RA, Hui HL, Andracki ME, Noble RW, Sligar SG, Walder JA, Walder RY., Biochemistry 31(36), 1992
PMID: 1390646
Protein folding and its implications for the production of recombinant proteins.
Hlodan R, Craig S, Pain RH., Biotechnol. Genet. Eng. Rev. 9(), 1991
PMID: 1797019

AUTHOR UNKNOWN, 0

Keil, 1992
Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation.
Kiefhaber T, Rudolph R, Kohler HH, Buchner J., Biotechnology (N.Y.) 9(9), 1991
PMID: 1367356
Proteolytic response to the expression of an abnormal beta-galactosidase in Escherichia coli.
Kosinski MJ, Rinas U, Bailey JE., Appl. Microbiol. Biotechnol. 37(3), 1992
PMID: 1368906
Stabilization of recombinant proteins from proteolytic degradation in Escherichia coli using a dual affinity fusion strategy.
Murby M, Cedergren L, Nilsson J, Nygren PA, Hammarberg B, Nilsson B, Enfors SO, Uhlen M., Biotechnol. Appl. Biochem. 14(3), 1991
PMID: 1777118
Secretion incompetence of bovine pancreatic trypsin inhibitor expressed in Escherichia coli.
Nilsson B, Berman-Marks C, Kuntz ID, Anderson S., J. Biol. Chem. 266(5), 1991
PMID: 1704370
Cell-free translation systems may provide new bioprocessing techniques
Orr, Gen. Eng. News (), 1989
Cell-free translation systems may provide new bioprocessing techniques
Orr, Gen. Eng. News (), 1989
Sequence-specific cleavage of protein fusions using a recombinant Neisseria type 2 IgA protease.
Pohlner J, Klauser T, Kuttler E, Halter R., Biotechnology (N.Y.) 10(7), 1992
PMID: 1368270
High-level temperature-induced synthesis of an antibody VH-domain in Escherichia coli using the PelB secretion signal.
Power BE, Ivancic N, Harley VR, Webster RG, Kortt AA, Irving RA, Hudson PJ., Gene 113(1), 1992
PMID: 1563636
Cysteine to serine substitutions in basic fibroblast growth factor: effect on inclusion body formation and proteolytic susceptibility during in vitro refolding.
Rinas U, Tsai LB, Lyons D, Fox GM, Stearns G, Fieschko J, Fenton D, Bailey JE., Biotechnology (N.Y.) 10(4), 1992
PMID: 1368488
In-vitro cleavage of a fusion protein bound to cellulose using the soluble yscFs (Kex2) variant.
Seeboth PG, Warren RA, Heim J., Appl. Microbiol. Biotechnol. 37(5), 1992
PMID: 1368916
A pH regulated promoter for the expression of recombinant proteins in Escherichia coli
Tolentino, Biotechnol. Lett. 14(), 1992
Antibody engineering: the use of Escherichia coli as an expression host.
Ward ES., FASEB J. 6(7), 1992
PMID: 1563594
Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes.
Studier FW, Moffatt BA., J. Mol. Biol. 189(1), 1986
PMID: 3537305
Construction of an Escherichia coli export-affinity vector for expression and purification of foreign proteins by fusion to cyclomaltodextrin glucanotransferase.
Hellman J, Mantsala P., J. Biotechnol. 23(1), 1992
PMID: 1368771
Protein release in recombinant Escherichia coli using bacteriocin release protein.
Yu P, San KY., Biotechnol. Prog. 8(1), 1992
PMID: 1367893
Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 14544808
PubMed | Europe PMC

Suchen in

Google Scholar