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...

Full description

Saved in:
Bibliographic Details
Published in:Appl Environ Microbiol
Main Authors: Mitchell, P, Yen, H C, Mathemeier, P F
Format: Artigo
Language:Inglês
Published: American Society for Microbiology (ASM) 1985
Subjects:
Research Article
Online Access: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
Tags: Add Tag
No Tags, Be the first to tag this record!

Similar Items