title: Association of creatine kinase with rat heart mitochondria: high and low affinity binding sites and the involvement of phospholipids.
abstract: Cleavage of mitochondrial phosphatidylethanolamine (PE), phosphatidylcholine (PC) and cardiolipin (CL) by phospholipase A2 but not selective degradation of PE and PC by phospholipase C dissociates creatine kinase from rat heart mitochondria. Creatine kinase exhibits a high resistance against Triton X-100 solubilization up to concentrations of 0.05-0.1%. Scatchard plot of rebinding experiments using mitoplasts revealed the presence of both low and high affinity binding sites; the latter may account for the originally bound creatine kinase activity. It is suggested that creatine kinase is specifically bound to a CL containing domain of the inner mitochondrial membrane.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002308:Cardiolipins / Q000378:metabolism; D003402:Creatine Kinase / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D008929:Mitochondria, Heart / Q000378:metabolism*; D010713:Phosphatidylcholines / Q000378:metabolism; D010714:Phosphatidylethanolamines / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism*; D051381:Rats; D012995:Solubility
chemical_list: D002308:Cardiolipins; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D010743:Phospholipids; D003402:Creatine Kinase