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Identification of the site phosphorylated by casein kinase II in smooth muscle caldesmon
Author(s) -
Wawrzynow Alicja,
Collins John H.,
Bogatcheva Natalia V.,
Vorotnikov Alexander V.,
Gusev Nikolai B.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81072-g
Subject(s) - caldesmon , casein kinase 2 , phosphorylation , identification (biology) , chemistry , biochemistry , binding site , protein kinase a , biophysics , biology , calmodulin , mitogen activated protein kinase kinase , enzyme , botany
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 Cys 153 . 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, Ser 73 is the main site phosphorylated by casein kinase II in avian gizzard caldesmon.