title: [The effect of media pH and autocatalytic phosphorylation on the interaction of kinase phosphorylase with calmodulin].
abstract: Using calmodulin covalently labeled with dansyl, the Ca2(+)-dependent interaction of phosphorylase kinase with calmodulin has been studied. It has been shown that at pH 6.8 the (alpha beta gamma delta) protomer of the enzyme binds 2.1 +/- 0.8 mol of calmodulin with Kd = (6.67 +/- 1.77).10(-8) M. The enzyme activation induced by the pH increase up to 8.2 does not affect the enzyme interaction with calmodulin [2.14 +/- 0.58 mol calmodulin per mol of (alpha beta gamma delta)]; Kd = (4.14 +/- 1.22).10(-8) M. However, the enzyme activation during its autocatalytic phosphorylation eliminates this effect practically completely.
authors.forename: A E
authors.initials: AE
authors.lastname: Goldshteĭn
authors.forename: S A
authors.initials: SA
authors.lastname: Shur
authors.forename: I A
authors.initials: IA
authors.lastname: Feoktistov
mesh_terms: D000818:Animals; D002147:Calmodulin / Q000378:metabolism*; D002384:Catalysis; D006863:Hydrogen-Ion Concentration; D010764:Phosphorylase Kinase / Q000378:metabolism*; D010766:Phosphorylation; D011817:Rabbits; D013050:Spectrometry, Fluorescence
chemical_list: D002147:Calmodulin; D010764:Phosphorylase Kinase
vernacular_title: Vliianie pH sredy i autokataliticheskogo fosforilirovaniia na vzaimodeĭstvie kinazy fosforilazy s kalmodulinom.