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Title: Phosphorylation in vitro of human fibrinogen with casein kinase TS and characterization of phosphorylated sites

Journal Article · · Arch. Biochem. Biophys.; (United States)

Human fibrinogen was phosphorylated by casein kinase TS. The (/sup 32/P)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.

Research Organization:
Biomedical Center, Uppsala, Sweden
OSTI ID:
5630148
Journal Information:
Arch. Biochem. Biophys.; (United States), Vol. 257:2
Country of Publication:
United States
Language:
English