title: Isolation and properties of creatine kinase from the breast muscle of tropical fruit bat, Eidolon helvum (Kerr).
abstract: Creatine kinase, from fruit bat breast muscle, has been purified to homogeneity. The mol. wt of the enzyme was estimated to be about 78,000-80,000 with two subunits of 42,500. There are nine thiol residues/mol of the enzyme and two of these react readily with DTNB leading to total inactivation of the enzyme. The metal ion specificity was in order Mg2+ greater than Zn2+ greater than Co2+. Initial velocity and product inhibition studies of the reverse reaction are consistent with sequential reaction but of either rapid equilibrium random or ordered type.
mesh_terms: D000818:Animals; D002413:Cations, Divalent; D002685:Chiroptera / Q000378:metabolism*; D003402:Creatine Kinase / Q000302:isolation & purification / Q000378:metabolism*; D004228:Dithionitrobenzoic Acid / Q000494:pharmacology; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*
chemical_list: D002413:Cations, Divalent; D004228:Dithionitrobenzoic Acid; D003402:Creatine Kinase