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...
محفوظ في:
| الحاوية / القاعدة: | Appl Environ Microbiol |
|---|---|
| المؤلفون الرئيسيون: | , , |
| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
American Society for Microbiology (ASM)
1985
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| الموضوعات: | |
| الوصول للمادة أونلاين: | 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 |
| الوسوم: |
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