Phosphorylation of fibrinogen by casein kinase 1.
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 alpha-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.
D000818:Animals; D002118:Calcium / Q000378:metabolism; D047388:Casein Kinases; D002417:Cattle; D000242:Cyclic AMP / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000378:metabolism*; D006006:Glycogen Synthase / Q000378:metabolism; D006801:Humans; D008099:Liver / Q000201:enzymology; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
D005340:Fibrinogen; D000242:Cyclic AMP; D006006:Glycogen Synthase; D011494:Protein Kinases; D047388:Casein Kinases; D002118:Calcium