PMID: 2461739Dec 2, 1988Paper

Aprotinin derivatives with chromophoric leaving groups can be used as highly selective active-site titrants for serine proteinases and permit the determination of kinetic constants of enzyme-inhibitor complexes

Biochimica Et Biophysica Acta
A MehlichH Tschesche


This paper reports a novel and valuable approach to active-site titration. The starting substance for the preparation of the active-site titrants is aprotinin (bovine pancreatic trypsin inhibitor) in which the reactive-site peptide bond, Lys15-Ala16, is split. Two cystine disulfide bonds hold together the two peptide chains. The Lys15 of the reactive site is substituted by arginine-, phenylalanine- and valine-4-nitroanilide or by valine-7-amido-4-methylcoumarin. The different incorporated amino acid residues correspond to different specificities against serine proteinases. Serine proteinases with suitable specificity are able to remove 4-nitroaniline or 7-amino-4-methylcoumarin from these aprotinin derivatives while at the same time resynthesis of the reactive-site peptide bond occurs. The proteinase is then trapped in a stable enzyme-inhibitor complex, which prevents the proteinase from releasing further leaving groups. The quantity of 4-nitroaniline or 7-amino-4-methylcoumarin, which can be assayed spectrophotometrically or fluorometrically is equimolar to the quantity of proteinase used and trapped. The aprotinin derivatives with an incorporated Phe15 or Val15 residue are highly specific for chymotrypsin or for elastase from...Continue Reading


Jun 1, 1976·Hoppe-Seyler's Zeitschrift für physiologische Chemie·H Tschesche, S Kupfer
Jan 1, 1976·Methods in Enzymology·P L ColemanE N Shaw
May 27, 1987·Biochimica Et Biophysica Acta·H TschescheH R Wenzel
Apr 20, 1967·Biochemical and Biophysical Research Communications·I Schechter, A Berger
Mar 1, 1982·Hoppe-Seyler's Zeitschrift für physiologische Chemie·S EngelbrechtH Tschesche
Aug 15, 1984·Archives of Biochemistry and Biophysics·G OshimaM Yamada
Feb 15, 1983·Biochimica Et Biophysica Acta·R Lottenberg, C M Jackson
Jan 1, 1981·Methods in Enzymology·W F MangelH Y Liu
Nov 30, 1967·Biochemical and Biophysical Research Communications·T Chase, E Shaw

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