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. 1985 May;49(5):1232–1234. doi: 10.1128/aem.49.5.1332-1334.1985

Properties of lactate dehydrogenase in a psychrophilic marine bacterium.

P Mitchell, H C Yen, P F Mathemeier
PMCID: PMC238534  PMID: 4004236

Abstract

Lactate dehydrogenase (EC 1.1.1.27) from Vibrio marinus MP-1 was purified 15-fold and ammonium activated. The optimum pH for pyruvate reduction was 7.4. Maximum lactate dehydrogenase activity occurred at 10 to 15 degrees C, and none occurred at 40 degrees C. The crude-extract enzyme was stable between 15 and 20 degrees C and lost 50% of its activity after 60 min at 45 degrees C. The partially purified enzyme was stable between 8 and 15 degrees C and lost 50% of its activity after 60 min at 30 degrees C. The thermal stability of lactate dehydrogenase was increased by mercaptoethanol, with 50% remaining activity at 42 degrees C.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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