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 …

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 …

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 …

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

The action of serine (and cysteine) proteases on peptide esters proceeds, as a
generalization, orders of magnitude faster than the corresponding enzymatic hydrolysis of …

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 …

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 …

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 …

Serine Proteinases Mimics: Hydrolytic Activity of Cyclic Peptides Which Include a Non-natural
Amino Acid t Page 1 Tvrrnhrdrorl Lerreu, Vol. 36, No. 49. pp X987-8990, 1995 Elsevier Scmm …

In a new strategy for labeling the active sites of serine proteinases with fluorescence probes
(Bock, PE (1988) Biochemistry 27, 6633-6639), a thioester peptide chloromethyl ketone …