Structural and Functional Characterization of Calelectrins from Bovine Liver

概要

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Two Ca^<2+>-dependent membrane-binding proteins with apparent molecular weights of 70000 (calelectrin_<70>) and 32000 (calelectrin_<32>) were isolated from bovine liver using phenyl-Sepharose affinity chromatography followed by diethylaminoethyl (DEAE)-celllulose and Ultrogel AcA44 chromatographies. Limited proteolysis and immunological analyses indicated that calelectrin_<32> was not a digested product from calelectrin_<70>. Both calelectrins bound to phosphatidylserine and to calmodulin in a Ca^<2+>-dependent manner. Circular dichroism studies showed that the apparent α-helical contents of calelectrin_<70> and calelectrin_<32> were 25 and 40%, respectively and they underwent Ca^<2+> -dependent conformational changes. When the calelectrins were incubated with a brain microtubule preparation, they were phosphorylated by endogenous kinase(s) and phosphorylation occurred on serine residues. Moreover, calelectrin_<70> showed an inhibitory action on endogenous kinase activity in the presence of Ca^<2+>.
公益社団法人日本薬学会の論文
1991-02-25