Phosphorylation of the alpha-chain of fibrinogen by a platelet kinase activity enhanced by interferon.
Treatment of patients with interferon or inducers of interferon results in an enhanced level of a protein kinase activity found in platelets (1,3). The kinase activity is responsible for the phosphorylation of a 70-72,000 molecular weight protein (72K protein) found in blood plasma. By the means of a technique based on the precipitation of this protein kinase system (the protein kinase and its substrate), we show here that the 72K protein is the alpha-chain of fibrinogen. During the coagulation process induced by thrombin, the 32P-labelled 72K protein is recovered in the clot. After incubation in the presence of thrombin, the 72K protein looses a small polypeptide of 2-3000 in molecular weight resulting a shift in its isoelectric point (pI) from 6.8-7.0 to 7.5. At the end of the coagulation process, the 32P-labelled 72K protein becomes undetectable since it gives rise to a covalently linked alpha-polymer of a high molecular weight. In accord with these results, the 72K protein could be precipitated by antibodies against human fibrinogen.
D000906:Antibodies; D000936:Antigen-Antibody Complex; D001777:Blood Coagulation; D001792:Blood Platelets / Q000201:enzymology*; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D007372:Interferons / Q000494:pharmacology*; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000097:blood* / Q000302:isolation & purification; D013917:Thrombin / Q000378:metabolism
D000906:Antibodies; D000936:Antigen-Antibody Complex; D046911:Macromolecular Substances; D005340:Fibrinogen; D007372:Interferons; D011494:Protein Kinases; D013917:Thrombin