Effect of phosphorylation in vitro of human fibrinogen with protein kinase C on thrombin-induced gelation |
| |
Authors: | P Heldin B Hessel E Humble B Blomb?ck L Engstr?m |
| |
Affiliation: | Department of Physiological Chemistry, University of Uppsala, Sweden. |
| |
Abstract: | Thrombin-induced gel formation of fibrinogen phosphorylated by protein kinase C yielded a transparent gel, whereas unphosphorylated fibrinogen yielded a coarse gel. The mass-length ratio was found to be one order of magnitude higher for the unphosphorylated than for the phosphorylated fibrinogen. Since the phosphorylated sites are located near the cross-linking sites in the A alpha-chain of fibrinogen, it is likely that the introduction of charged phosphate groups in this region prevent the lateral growth of the fibrin fibres. |
| |
Keywords: | |
|
|