Properties of lactate dehydrogenase in a psychrophilic marine bacterium.
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 betwe...
Uloženo v:
| Vydáno v: | Appl Environ Microbiol |
|---|---|
| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1985
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC238534/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/4004236/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.49.5.1332-1334.1985 |
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