Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Polymorphism of the membrane proteinases of the mitochondria

Journal Article · · Biochemistry (Engl. Transl.); (United States)
OSTI ID:5767865
Three protein fractions capable of catalyzing the proteolysis of cytochrome c and three other fractions catalyzing the hydrolysis of N-..cap alpha..-benzoyl-L-arginine-p-nitroanilide (BAPA) and N-..cap alpha..-benzoyl-L-arginine-..beta..-naphthylamide (BANA) were separated by electrophoresis in polyacrylamide gel in the absence of SDS detergent extracts from ultrasonic submitochondrial particles (SMP). The indicated fractions were isolated from gel and studied according to a series of parameters. It was shown that cytochrome c hydrolases have the same molecular weight (17,000) but different isoelectric points (4.0, 4.2, and 4.4). The total cytochrome c hydrolase activity of these enzymes was inhibited by phenylmethylsulfonyl fluoride but was insensitive to ethylenediaminetetraacetate and o-phenanthroline. The three BANA (BAPA) hydrolases also had similar molecular weights (approx. 17,500) and different isoelectric points (4.2, 4.3, and 4.7). In addition to the indicated hydrolases, minor components, possessing the same activities but differing in strength of the bond to the inner mitochondrial membrane, molecular weight, and sensitivity to proteinase inhibitors, were detected in the detergent extracts of the SMP. It was concluded that there is a polymorphism of the proteinases associated with the inner mitochondrial membrane.
Research Organization:
M.V. Lomonosov Moscow State Univ., USSR
OSTI ID:
5767865
Journal Information:
Biochemistry (Engl. Transl.); (United States), Journal Name: Biochemistry (Engl. Transl.); (United States) Vol. 50:3; ISSN BIORA
Country of Publication:
United States
Language:
English