Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization
Mevarech M, Eisenberg H, Neumann E (1977)
Biochemistry 16(17): 3781-3785.
Zeitschriftenaufsatz
| Veröffentlicht | Englisch
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Autor*in
Mevarech, Moshe;
Eisenberg, Henryk;
Neumann, EberhardUniBi
Einrichtung
Stichworte
Molecular biology;
Biochemistry
Erscheinungsjahr
1977
Zeitschriftentitel
Biochemistry
Band
16
Ausgabe
17
Seite(n)
3781-3785
ISSN
0006-2960
eISSN
1520-4995
Page URI
https://pub.uni-bielefeld.de/record/1774414
Zitieren
Mevarech M, Eisenberg H, Neumann E. Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization. Biochemistry. 1977;16(17):3781-3785.
Mevarech, M., Eisenberg, H., & Neumann, E. (1977). Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization. Biochemistry, 16(17), 3781-3785. https://doi.org/10.1021/bi00636a009
Mevarech, Moshe, Eisenberg, Henryk, and Neumann, Eberhard. 1977. “Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization”. Biochemistry 16 (17): 3781-3785.
Mevarech, M., Eisenberg, H., and Neumann, E. (1977). Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization. Biochemistry 16, 3781-3785.
Mevarech, M., Eisenberg, H., & Neumann, E., 1977. Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization. Biochemistry, 16(17), p 3781-3785.
M. Mevarech, H. Eisenberg, and E. Neumann, “Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization”, Biochemistry, vol. 16, 1977, pp. 3781-3785.
Mevarech, M., Eisenberg, H., Neumann, E.: Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization. Biochemistry. 16, 3781-3785 (1977).
Mevarech, Moshe, Eisenberg, Henryk, and Neumann, Eberhard. “Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization”. Biochemistry 16.17 (1977): 3781-3785.
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Daten bereitgestellt von European Bioinformatics Institute (EBI)
32 Zitationen in Europe PMC
Daten bereitgestellt von Europe PubMed Central.
Salt-bridge energetics in halophilic proteins.
Nayek A, Sen Gupta PS, Banerjee S, Mondal B, Bandyopadhyay AK., PLoS ONE 9(4), 2014
PMID: 24743799
Nayek A, Sen Gupta PS, Banerjee S, Mondal B, Bandyopadhyay AK., PLoS ONE 9(4), 2014
PMID: 24743799
Protective role of salt in catalysis and maintaining structure of halophilic proteins against denaturation.
Sinha R, Khare SK., Front Microbiol 5(), 2014
PMID: 24782853
Sinha R, Khare SK., Front Microbiol 5(), 2014
PMID: 24782853
Characterization of malate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum.
Yennaco LJ, Hu Y, Holden JF., Extremophiles 11(5), 2007
PMID: 17487443
Yennaco LJ, Hu Y, Holden JF., Extremophiles 11(5), 2007
PMID: 17487443
Characteristic views of prokaryotic 50S ribosomal subunits.
Harauz G, Stoeffler-Meilicke M, van Heel M., J. Mol. Evol. 26(4), 1987
PMID: 3131536
Harauz G, Stoeffler-Meilicke M, van Heel M., J. Mol. Evol. 26(4), 1987
PMID: 3131536
Structure of halophilic malate dehydrogenase in multimolar KCl solutions from neutron scattering and ultracentrifugation.
Calmettes P, Eisenberg H, Zaccai G., Biophys. Chem. 26(2-3), 1987
PMID: 17010283
Calmettes P, Eisenberg H, Zaccai G., Biophys. Chem. 26(2-3), 1987
PMID: 17010283
The halophilic properties of pyruvate kinase from Vibrio costicola, a moderate halophile.
de Medicis E, Rossignol B., Experientia 35(12), 1979
PMID: 391582
de Medicis E, Rossignol B., Experientia 35(12), 1979
PMID: 391582
A comparative study on the stability of immobilized halophilic and non-halophilic malate dehydrogenases at various ionic strengths.
Koch-Schmidt AC, Mosbach K, Werber MM., Eur. J. Biochem. 100(1), 1979
PMID: 488091
Koch-Schmidt AC, Mosbach K, Werber MM., Eur. J. Biochem. 100(1), 1979
PMID: 488091
References
Daten bereitgestellt von Europe PubMed Central.
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