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

FEBS Letters

Gusev, Nikolai B.²  Collins, John H.¹  Vorotnikov, Alexander V.²  Wawrzynow, Alicja¹  Bogatcheva, Natalia V.² 

[1]Department of Biological Chemistry, School of Medicine and Medical Biotechnology Center, Maryland Biotechnology Institute, University of Maryland, Baltimore, MD 21201, USA

[2]Department of Biochemistry, School of Biology, Moscow State University, Moscow 119899, USSR

关键词: Caldesmon;    Casein kinase II;    Phosphorylation;   

DOI  :  10.1016/0014-5793(91)81072-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 M _r, 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 phosphorserine. Thus, Ser⁷³ is the main site phosphorylated by casein kinase II in avian gizzard caldesmon.

【 授权许可】

Unknown