Phosphorylation in vitro of human fibrinogen with casein kinase TS and characterization of phosphorylated sites.
Human fibrinogen was phosphorylated by casein kinase TS. The [32P]phosphate incorporated varied between 0.5 and 1 mol of phosphate per mole of fibrinogen. The phosphate was localized to Ser523 and Ser590 and serine and threonine residues between amino acids 259 and 268 in the A alpha-chain. In addition, Thr416 and Ser420 were phosphorylated in the gamma'-chain, which is a variant of the gamma-chain, constituting 7-10% of the gamma-chain population. The functional significance of casein kinase TS-induced phosphorylation of fibrinogen remains unknown; however, a slight but consistent increase of the turbidity in a gelation assay was observed for phosphorylated compared to unphosphorylated fibrinogen.
D047388:Casein Kinases; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010748:Phosphopeptides / Q000032:analysis; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D014357:Trypsin
D010446:Peptide Fragments; D010748:Phosphopeptides; D010761:Phosphorus Radioisotopes; D005340:Fibrinogen; D011494:Protein Kinases; D047388:Casein Kinases; D002918:Chymotrypsin; D014357:Trypsin; D003488:Cyanogen Bromide