Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure

Mevarech M, Neumann E (1977)
Biochemistry 16(17): 3786-3792.

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Biochemistry
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3786-3792
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Mevarech M, Neumann E. Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry. 1977;16(17):3786-3792.
Mevarech, M., & Neumann, E. (1977). Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry, 16(17), 3786-3792. doi:10.1021/bi00636a010
Mevarech, M., and Neumann, E. (1977). Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry 16, 3786-3792.
Mevarech, M., & Neumann, E., 1977. Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry, 16(17), p 3786-3792.
M. Mevarech and E. Neumann, “Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure”, Biochemistry, vol. 16, 1977, pp. 3786-3792.
Mevarech, M., Neumann, E.: Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry. 16, 3786-3792 (1977).
Mevarech, Moshe, and Neumann, Eberhard. “Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure”. Biochemistry 16.17 (1977): 3786-3792.
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17 Zitationen in Europe PMC

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Hydration shells with a pinch of salt.
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PMID: 23348670
Genes from Debaryomyces hansenii increase salt tolerance in Saccharomyces cerevisiae W303.
Prista C, Soeiro A, Vesely P, Almagro A, Ramos J, Loureiro-Dias MC., FEMS Yeast Res. 2(2), 2002
PMID: 12702302
Halophilic enzymes: proteins with a grain of salt.
Mevarech M, Frolow F, Gloss LM., Biophys. Chem. 86(2-3), 2000
PMID: 11026680
Expression of Batis maritima methyl chloride transferase in Escherichia coli.
Ni X, Hager LP., Proc. Natl. Acad. Sci. U.S.A. 96(7), 1999
PMID: 10097085
Halophilic proteins and the influence of solvent on protein stabilization.
Zaccai G, Eisenberg H., Trends Biochem. Sci. 15(9), 1990
PMID: 2238041
Stabilization of halophilic malate dehydrogenase.
Zaccai G, Cendrin F, Haik Y, Borochov N, Eisenberg H., J. Mol. Biol. 208(3), 1989
PMID: 2795658
Crystallization of halophilic malate dehydrogenase from Halobacterium marismortui.
Harel M, Shoham M, Frolow F, Eisenberg H, Mevarech M, Yonath A, Sussman JL., J. Mol. Biol. 200(3), 1988
PMID: 3398050
Polypeptide elongation factor Tu from Halobacterium marismortui.
Guinet F, Frank R, Leberman R., Eur. J. Biochem. 172(3), 1988
PMID: 3127212

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