Activation of grass carp liver alcohol dehydrogenase by limited proteolysis
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AbstractLimited proteolysis of grass carp alcohol dehydrogenase by alkaline protease or subtilisin BPN' at 30 degrees C for 6 hr generated a nicked species that was catalytically active. Electrophoresis on a denaturing SDS-PAGE showed that the 40 kDa subunit of the intact enzyme was cleaved to produce subunits of 27 and 13 kDa, which remained tightly associated with each other under native condition. Such a proteolytically nicked form was catalytically more active than the original intact form of the enzyme. The V-max value toward the oxidation of ethanol at pH 10 increased by 7.8 fold whereas the K-m value also exhibited a 140 fold increase. On the other hand, when the same protease treatment was applied to horse liver alcohol dehydrogenase, no activation nor any specific cleavage can be observed.
All Author(s) ListLau KK, Fong WP
Journal nameBIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL
Year1996
Month12
Day1
Volume Number40
Issue Number6
PublisherACADEMIC PRESS AUST
Pages1095 - 1103
ISSN1039-9712
LanguagesEnglish-United Kingdom
Keywordsactivation; alcohol dehydrogenase; grass carp; proteolysis
Web of Science Subject CategoriesBiochemistry & Molecular Biology

Last updated on 2020-03-04 at 00:56