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- W141846990 abstract "Three Threonyl and at least six Seryl residues phosphorylated in five different model protein substrates by Caseinkinase TS (CK-TS), a cAMP-independent proteinkinase whose function in the rat liver cytosol is still obscure, have been identified. All of them are located at the N terminal side of two or more acidic residues, within segments having an high probability of occurrence as β-turns. Most of the Phosphoseryl residues of native caseins display the same features. Moreover all the four typical (Ser-P)3 clusters of αs1, αs2, and β-caseins can be phosphorylated also by CK-TS after partial dephosphorylation. CNBr and Trypsin digestion of αs2-casein promotesa remarkable fall of the phosphorylation rate of residues still included in relatively large peptides, suggesting that the CK-TS activity might be optimized by a definite size or shape of the protein substrate. The striking specificity of the “so-called” rat liver Casein kinase TS for the same sites phosphorylated in vivo by the “true” mammary gland Caseinkinase suggests as a working hypothesis that these two enzymes, though playing different roles, might be related to each other." @default.
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- W141846990 date "1980-01-01" @default.
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- W141846990 title "STRUCTURAL REQUIREMENTS OF A RAT LIVER PROTEINKINASE DISPLAYING A SPECIFICITY SIMILAR TO THAT OF THE MAMMARY GLAND CASEINKINASE(S)" @default.
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- W141846990 doi "https://doi.org/10.1016/b978-0-08-024417-4.50008-1" @default.
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