Activation of grass carp liver alcohol dehydrogenase by limited proteolysis
نویسندگان
چکیده
منابع مشابه
Activation of rat liver microsomal glutathione transferase by limited proteolysis.
The activity of rat liver microsomal glutathione transferase is increased by limited tryptic proteolysis; the membrane-bound and purified forms of the enzyme are activated about 5- and 10-fold respectively. The cleavage sites that correlate with this activation were determined by amino acid sequence analysis to be located after Lys-4 and Lys-41. Differences in the relative extent of cleavage at...
متن کاملProbing Conformational Feature of a Recombinant Pyruvate Kinase by Limited Proteolysis
Pyruvate kinase is a key enzyme in glycolytic pathway that catalyzes the transphosphorylation between phosphoenolpyruvate and ADP to yield ATP and Pyruvate. Geobacillus stearothermophillus has a stable pyruvate kinase with determined crystal structure that composed of four separate domains. Given that limited proteolysis experiments can be successfully used to probe conformational features of p...
متن کاملMolecular characterization of glutathione peroxidase gene from the liver of silver carp, bighead carp and grass carp.
The cDNAs encoding glutathione peroxidase (GPx) were cloned and sequenced from the liver of three Chinese carps with different tolerance to hepatotoxic microcystins, phytoplanktivorous silver carp (Hypophthalmichthys molitrix) and bighead carp (Aristichthys nobilis), and herbivorous grass carp (Ctenopharyngodon idellus). Using genome walker method, a 750 bp 5'-flanking region of the silver carp...
متن کاملReversible Oxidation of Cyclic Secondary Alcohols by Liver Alcohol Dehydrogenase
During a study of cyclic alcohol oxidation by a partially purified rat liver enzyme system (l), it was noted that ethanol was also oxidized by this preparation. Since the ratio of the rate of ethanol oxidation to the rate of cyclohexanol oxidation remained constant during purification, the possibility arose that the activity with cyclic substrates was due to the conventional alcohol dehydrogena...
متن کاملThe dismutation of formaldehyde by liver alcohol dehydrogenase.
The results obtained led the authors to the suggestion that Reactions 2 and 4 are catalyzed by liver alcohol dehydrogenase but that Reaction 1 is due to an aldehyde dehydrogenase present in their liver preparation. Because of the inhomogeneity of the enzyme preparation employed, a reinvestigation of this problem with more highly purified enzyme was suggested. With the use of crystalline horse l...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: IUBMB Life
سال: 1996
ISSN: 1521-6543
DOI: 10.1080/15216549600201733