Proteolytic fragmentation of fibrinogen. II. kinetic modeling of the digestion of human and bovine fibrinogen plasmin or trypsin.
The kinetic data presented in the previous paper (Mihalyi, E., et al. (1976), Biochemistry 15, preceding paper in this issue), with respect to the fragmentation of human the bovine fibrinogen by either plasmin or trypsin, were compared with several chemical kinetic models. The models were derived mathematically on the basis of the three-nodular  structure of fibrinogen (Hall, C.E., and Sayter, H.S. (1959), J. BiophysBiochem. Ctyol. 5, 11) and the asymmetrical cleavage sequence first proposed by Marder, V.J., et. al. ((1969) J. Biol. Chem. 244, 2111). The parameters were determined by nonlinear curve fitting. The whole process could be described accurately by only two rate constants. Several variant models were tested and, although a clear cut choice cannot be made,  one of these, the protected three-bonds model, appears to give the best fit in most cases. This model assumes that the chain segment that distinguishes F from X protects certain other chains (the bonds) from proteolytic cleavage.
D000818:Animals; D002417:Cattle; D005340:Fibrinogen / Q000378:metabolism*; D005341:Fibrinolysin / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008954:Models, Biological; D014357:Trypsin / Q000378:metabolism*
D005340:Fibrinogen; D014357:Trypsin; D005341:Fibrinolysin