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By lengthening the sequence of a previously available tripeptide to a pentapeptide, we were able to increase the specificity of the substrate for the complement enzyme CVFBb (EC 3.4.21.47) over Factor Xa (EC 3.4.21.6). This increase in specificity was achieved by both an increase in the kcat/Km for CVFBb for the longer substrate compared to the original substrate, and a decrease in the kcat/Km for Factor Xa. The new substrate, Boc-Nle-Gln-Leu-Gly-Arg-amino methyl coumarin (AMC) was synthesized by coupling Boc-Nle-Gln-Leu-Gly to Arg-AMC in solution. p-Toluenesulfonic acid was added to the coupling mixture to improve the solubility of the arginine derivative and avoid the need for covalent protection.
J C Gutierrez, and
O Götze, and
L H Caporale
July 1981,
Biochimica et biophysica acta,
J C Gutierrez, and
O Götze, and
L H Caporale
November 1977,
Analytical biochemistry,
J C Gutierrez, and
O Götze, and
L H Caporale
September 1978,
Clinical chemistry,
J C Gutierrez, and
O Götze, and
L H Caporale
December 1987,
Journal of immunological methods,
J C Gutierrez, and
O Götze, and
L H Caporale
May 1999,
Immunopharmacology,
J C Gutierrez, and
O Götze, and
L H Caporale
November 1975,
Journal of immunology (Baltimore, Md. : 1950),
J C Gutierrez, and
O Götze, and
L H Caporale
January 1991,
Peptide research,
J C Gutierrez, and
O Götze, and
L H Caporale
April 2013,
Bioorganic & medicinal chemistry letters,
J C Gutierrez, and
O Götze, and
L H Caporale
April 1985,
Analytical biochemistry,
J C Gutierrez, and
O Götze, and
L H Caporale
August 2013,
Proceedings of the National Academy of Sciences of the United States of America,
