Phosphorylation of fibrinogen by casein kinase 1

E. Itarte, M. Plana, M. D. Guasch, C. Martos

Research output: Contribution to journalArticleResearchpeer-review

15 Citations (Scopus)


Casein kinase 1 phosphorylated human fibrinogen, in a reaction that did not use GTP as phosphoryl donor and was neither stimulated by cyclic AMP or Ca2+, nor inhibited by the cyclic AMP-dependent protein kinase inhibitor protein. Maximal incorporation averaged 4 mol of phosphate per mol of fibrinogen, most of it in the largest CNBr-fragment of the α-chain. Phosphoamino acid analysis revealed that phosphorylation occurred only at seryl residues. The phosphorylation of fibrinogen by casein kinase 1 was reverted by alkaline phosphatase. © 1983.
Original languageEnglish
Pages (from-to)631-636
JournalBiochemical and Biophysical Research Communications
Publication statusPublished - 16 Dec 1983


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