Role of fibrinopeptide B release: comparison of fibrins produced by thrombin and Ancrod.
The gelation time, opacity, light scattering, and elastic moduli of human fibrin gels clotted in the presence of thrombin, Ancrod, and Reptilase have been compared. At low ionic strength lateral association to thick fibers is observed in all cases. At all ionic strengths thrombin fibrin forms thicker fibers than does Ancrod fibrin. We have demonstrated that an increase in the extent of lateral association is linked to an increase in its velocity and to a decrease in the gelation time. One may consider the removal of fibrinopeptide B to act as a switch: after it is removed fibrin assembles rapidly to thick fibers and gelation is fast; but when this peptide is still attached, there is a slow assembly of thin fibers, and gelation, especially of dilute fibrin, is delayed. We believe that this delay is critical for the complete digestion by plasmin of fibrin formed during in vivo defibrination with  Ancrod and of fibrin produced by very small amounts of thrombin (which would still contain fibrinopeptide B), and that slow release of fibrinopeptide B is part of a control mechanism for the regulation of fibrin formation and the prevention of intravascular coagulation.
D000721:Ancrod / Q000378:metabolism*; D012103:Batroxobin / Q000378:metabolism*; D002118:Calcium / Q000494:pharmacology; D004548:Elasticity; D010450:Endopeptidases / Q000378:metabolism*; D005337:Fibrin; D005340:Fibrinogen / Q000378:metabolism; D005345:Fibrinopeptide B / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008027:Light; D009391:Nephelometry and Turbidimetry; D009994:Osmolar Concentration; D010447:Peptide Hydrolases / Q000378:metabolism*; D011487:Protein Conformation; D012542:Scattering, Radiation; D013917:Thrombin / Q000378:metabolism*
D005345:Fibrinopeptide B; D005337:Fibrin; D005340:Fibrinogen; D010450:Endopeptidases; D010447:Peptide Hydrolases; D000721:Ancrod; D012103:Batroxobin; D013917:Thrombin; D002118:Calcium