Dephosphorylation of human fibrinogen, previously phosphorylated in vitro by protein kinase C, by whole blood or intestinal alkaline phosphatase. Effects on thrombin-induced gelation of in vitro dephosphorylated human fibrinogen.
Human fibrinogen, a phosphoprotein, was either left untreated or phosphorylated by protein kinase C. Then both were dephosphorylated by calf intestinal alkaline phosphatase. The dephosphorylated fibrinogen gave an increased fibre thickness during thrombin-induced gelation. Whole blood anticoagulated by heparin, EDTA or sodium citrate, contained dephosphorylating activity against 32P-labeled fibrinogen, although there were significant differences in activity among the three anticoagulants.
Forsberg
P O
PO
Department of Medical and Physiological Chemistry, University of Uppsala, Sweden.
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D001769:Blood; D002417:Cattle; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007422:Intestines / Q000201:enzymology; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D013917:Thrombin / Q000494:pharmacology
D005340:Fibrinogen; D011493:Protein Kinase C; D000469:Alkaline Phosphatase; D013917:Thrombin