A microassay based on fluorescence resonance energy transfer has been developed to
determine the S′ specificity of serine proteases. The protease-catalyzed acyl transfer from …

Publisher Summary This chapter focuses on the thioester peptide chloromethyl ketones that
are the reagents for active site-selective labeling of serine proteinases with spectroscopic …

Publisher Summary Serine proteases are involved in a wide variety of biological reactions.
Sensitive assays for these enzymes are needed because in many cases they are present in …

MATERIALS AND METHODS Enzymes. Bovine-chymotrypsin (lyophilized, analytical grade,
lot 10860521-39, Boehringer, Mannheim, Germany) and bovinetrypsin (lyophilized …

In this paper we present an HPLC method developed for quick activity and specificity
analysis of serine proteinases. The method applies a carefully designed peptide library in …

Revised Manuscript Received April 4, 1988 abstract: The feasibility of a new approach to
incorporation of spectroscopic probes into the active sites of certain serine proteases has …

Chemical synthesis, physicochemical characterization and kinetic investigations of a
tetrapeptide library of chromogenic substrates containing the amide of 5-amino …

A series of dipeptide derivatives of Rhodamine, each containing an arginine residue in the
P1 position and one of ten representative benzyloxycarbonyl (Cbz)-blocked amino acids in …

We developed sensitive substrates for cysteine proteases and specific substrates for serine
proteases based on short internally quenched fluorescent peptides, Abz-FRX-EDDnp …

A new fluorogenic substrate for serine proteinases, bis (N-benzyloxycarbonyl-L-
argininamido) Rhodamine [(Cbz-Arg-NH) 2-Rhodamine], was synthesized, purified and …