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The activation of bovine coagulation factor X has been studied by kinetic and spectrophotometric measurements. The pH dependence of the hydrolysis of specific ester substrates by activated factor Xa can be ascribed to two independently ionizing groups with pKa values of 6.9 and 8.8, respectively. The rates of reaction of factor X, before and after activation, with the active-site titrant methanesulfonyl fluoride, suggest that the reactivity of the active-site serine residue in factor X is similar to that in trypsinogen and in factor Xa similar to that in trypsin. Analogous comparisons using diisopropyl phosphofluoridate as the titrant suggest that a hydrophobic binding site is absent in both the enzyme and zymogen. This conclusion is consistent with the lack of change in circular dichroism when acyl derivatives of factor V are converted to their acyl enzyme counterparts.
M A Kerr, and
D T Grahn, and
K A Walsh, and
H Neurath
January 1976,
Methods in enzymology,
M A Kerr, and
D T Grahn, and
K A Walsh, and
H Neurath
September 1975,
Proceedings of the National Academy of Sciences of the United States of America,
M A Kerr, and
D T Grahn, and
K A Walsh, and
H Neurath
December 1974,
Biochemistry,
M A Kerr, and
D T Grahn, and
K A Walsh, and
H Neurath
December 1972,
Biochemistry,
M A Kerr, and
D T Grahn, and
K A Walsh, and
H Neurath
March 1971,
Biulleten' eksperimental'noi biologii i meditsiny,
M A Kerr, and
D T Grahn, and
K A Walsh, and
H Neurath
August 2000,
Biochemistry,
M A Kerr, and
D T Grahn, and
K A Walsh, and
H Neurath
December 1972,
Biochemistry,
M A Kerr, and
D T Grahn, and
K A Walsh, and
H Neurath
October 1974,
FEBS letters,
M A Kerr, and
D T Grahn, and
K A Walsh, and
H Neurath
December 1972,
Biochemistry,
M A Kerr, and
D T Grahn, and
K A Walsh, and
H Neurath
February 1974,
Proceedings of the National Academy of Sciences of the United States of America,
