-transparent.png){kind=logo}
The time-dependent release by human alpha-thrombin of the physiological variants of fibrinopeptide A, i.e. fibrinopeptide A-3-phosphate (FPAP) and des-Ala-fibrinopeptide A (FPAY), has been measured in order to study the kinetic pathway for their hydrolysis. The best-fit kinetic model for the release of FPAP and FPAY is consistent with a simple pseudo first-order reaction, as observed with FPA. These findings indicate that FPAP and FPAY are also released from intact fibrinogen before release of FPB. The values of the specificity constants, i.e. k(at)/Km, for the enzymatic reaction between thrombin and the various alpha-chains showed that AP alpha- and AY alpha-chain are hydrolyzed with a 0.2-and 0.4-fold higher specificity constant respectively than that of A alpha-chain. Such minor differences observed with the various chains suggest that the 1-3 NH2-terminal residues of the chain do not significantly contribute to the catalytic efficiency of thrombin toward the alpha-chains of fibrinogen.
R De Cristofaro, and
M Castagnola
April 1996,
Biochemistry,
R De Cristofaro, and
M Castagnola
January 1967,
Acta chemica Scandinavica,
R De Cristofaro, and
M Castagnola
January 1990,
Medicina (Florence, Italy),
R De Cristofaro, and
M Castagnola
February 1988,
Biochemistry,
R De Cristofaro, and
M Castagnola
March 1975,
Thrombosis research,
R De Cristofaro, and
M Castagnola
January 1993,
Methods in enzymology,
R De Cristofaro, and
M Castagnola
April 1983,
Thrombosis research,
R De Cristofaro, and
M Castagnola
December 1989,
Proceedings of the National Academy of Sciences of the United States of America,
R De Cristofaro, and
M Castagnola
September 1974,
Thrombosis et diathesis haemorrhagica,
R De Cristofaro, and
M Castagnola
January 1968,
Acta physiologica Scandinavica. Supplementum,
