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Identification of the site phosphorylated by casein kinase II in smooth muscle caldesmon.

作者信息

Wawrzynow A, Collins J H, Bogatcheva N V, Vorotnikov A V, Gusev N B

机构信息

Department of Biological Chemistry, School of Medicine, University of Maryland, Baltimore 21201.

出版信息

FEBS Lett. 1991 Sep 9;289(2):213-6. doi: 10.1016/0014-5793(91)81072-g.

Abstract

Phosphorylation of avian gizzard caldesmon by casein kinase II was investigated. The enzyme incorporates about 1 mol of phosphate per mol of caldesmon. All sites of phosphorylation are located in short chymotryptic peptides with Mr 25-27 kDa or in the short N-terminal peptide formed after cleavage of chicken gizzard caldesmon at Cys153. The primary structure of the tryptic peptide containing the main site of duck gizzard caldesmon phosphorylation is S-E-V-N-A-Q-N-X-V-A-E-D-E-T-K, where X is an unidentified residue, presumed to be phosphoserine. Thus, Ser73 is the main site phosphorylated by casein kinase II in avian gizzard caldesmon.

摘要

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