Creatine kinase of heart mitochondria: no changes in its kinetic properties after inhibition of the adenine nucleotide translocator.
The kinetic properties of heart mitochondrial creatine kinase were measured with and without inhibitors of the adenine nucleotide translocator. No significant differences were observed suggesting that mitochondrial creatine kinase is not acting together with the adenine nucleotide translocator as a functional multienzyme complex. Adenine nucleotides from the bulk phase are able to enter the active center of creatine kinase without the necessity of transport via the adenine nucleotide translocator.
D000818:Animals; D001278:Atractyloside / Q000031:analogs & derivatives / Q000494:pharmacology*; D003402:Creatine Kinase / Q000378:metabolism*; D006027:Glycosides / Q000494:pharmacology*; D007700:Kinetics; D008929:Mitochondria, Heart / Q000201:enzymology*; D000226:Mitochondrial ADP, ATP Translocases / Q000037:antagonists & inhibitors*; D009713:Nucleotidyltransferases / Q000037:antagonists & inhibitors*; D051381:Rats
D006027:Glycosides; D001278:Atractyloside; D000226:Mitochondrial ADP, ATP Translocases; D003402:Creatine Kinase; D009713:Nucleotidyltransferases; C003853:carboxyatractyloside