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. 1980 Dec 1;191(3):851–854. doi: 10.1042/bj1910851

Phosphorylase kinase phosphorylation of skeletal-muscle troponin T.

V V Risnik, A B Dobrovolskii, N B Gusev, S E Severin
PMCID: PMC1162285  PMID: 7283976

Abstract

Rabbit skeletal-muscle troponin T was phosphorylated by a standard preparation of phosphorylase kinase [Cohen (1973) Eur. J. Biochem. 34, 1--14] and by fractions obtained after chromatography of phosphorylase kinase on phosphocellulose. The original preparation of phosphorylase kinase phosphorylated at least two sites, one of which was serine-1. The second and probably the third sites were presumably located in the peptide flanked by amino-acid residues 147 and 161 of troponin T. Fractions of phosphorylase kinase was adsorbed on phosphocellulose phosphorylated only the second site. Tightly adsorbed fractions possessed high troponin T kinase and phosvitin kinase activities and phosphorylated only serine-1 of troponin T. The results suggest that standard preparations of phosphorylase kinase are contaminated by troponin T kinase, which can phosphorylate serine-1 of troponin T.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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