Open AccessCatalatic activity of yeast cytochrome b 2 : l ‐lactate dehydrogenase
Author(s) -
Bhatti A.R.,
Seah T.C.M.,
Kaplan J.G.
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01394.x
Subject(s) - catalase , yeast , biochemistry , lactate dehydrogenase , cytochrome , chemistry , enzyme , cytochrome c , cytochrome c peroxidase , dehydrogenase , mitochondrion
Crude extracts of yeast exhibited two catalase activity bands on starch gel zymograms. Antibody prepared against catalase T specifically precipitated the fast‐moving catalatic band of catalase T, but did not affect the slow‐moving catalatic band of cytochrome b 2 . 3‐Amino‐1,2,4,‐triazole, a specific inhibitor of catalase, inhibited the catalytic activity of cytochrome b 2 but had little effect on its l ‐lactate dehydrogenase activity.