Phosphorylation of fibrinogen by casein kinase 2

M. D. Guasch, M. Plana, J. M. Pena, E. Itarte

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14 Citations (Scopus)

Abstract

Casein kinase 2 from rat liver cytosol phosphorylated human fibrinogen in a reaction that was not stimulated by Ca2+ or cyclic AMP, but was markedly inhibited by heparin, and proceeded at a similar rate when either ATP or GTP was used as phosphate donor. Analysis of casein kinase 2 by glycerol-density-gradient centrifugation showed that the activities towards fibrinogen, casein, phosvitin, high-mobility-group protein 14 and glycogen synthase coincided. Maximal incorporation into fibrinogen by casein kinase 2 averaged 1 mol of phosphate/mol of protein substrate, most of it in the α-chain, although some phosphorylation of the β-chain was also detected. Analysis of phosphorylated α-chain revealed that most of the phosphate was incorporated on serine. Phosphorylation of human fibrinogen was also performed by casein kinase 2 from human polymorphonuclear leucocytes, lymphocytes and platelets.
Original languageEnglish
Pages (from-to)523-526
JournalBiochemical Journal
Volume234
Issue number3
DOIs
Publication statusPublished - 1 Jan 1986

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