The appearance of a 34,000-dalton inhibitor of calpain (Ca2+-dependent cysteine proteinase) in rat liver after the administration of phenylhydrazine.
A 34,000-dalton inhibitor of calpain (Ca2+-dependent cysteine proteinase) was found in the cytosol of anemic rat liver. When phenylhydrazine hydrochloride was continuously administered to rats, a 280,000-dalton calpain inhibitor that existed originally in the liver gradually disappeared within two weeks and, concomitantly, a 34,000-dalton inhibitor appeared. The purified 34,000-dalton inhibitor resembles 280,000-dalton inhibitor in that both are heat-stable proteins and do not inhibit papain and trypsin. Unlike the protomers of a 280,000-dalton inhibitor, 34,000-dalton inhibitor does not show any sign of self-association.
D000740:Anemia / Q000378:metabolism; D000818:Animals; D002154:Calpain; D008099:Liver / Q000032:analysis / Q000187:drug effects*; D008297:Male; D008970:Molecular Weight; D010659:Phenylhydrazines / Q000494:pharmacology*; D011480:Protease Inhibitors; D051381:Rats; D011919:Rats, Inbred Strains; D014020:Tissue Extracts / Q000494:pharmacology*
D010659:Phenylhydrazines; D011480:Protease Inhibitors; D014020:Tissue Extracts; C030299:phenylhydrazine; D002154:Calpain