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 …

The behavior of an array of fluorescent human alpha-thrombin derivatives in reporting
binding of the fragment 2 domain of prothrombin was characterized as a representative …

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 …

Publisher Summary Amino acid chromogenic and fluorogenic substrates have been used for
many years for assaying proteases. The sensitivity of the assay procedures that employ …

Human α-and γ-thrombins were covalently labeled with two active serine directed probes,
dansyl fluoride and p-nitrophenyl anthranilate. Both probes inactivated the enzyme upon …

To assess the thrombin specificity of tripeptide chromogenic substrates, we determined the
Michaelis--Menten (Km), catalytic (kcat), and specificity (kcat/Km) constants for S-2238 (HD …

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 …

Native a-thrombin, the end product of the clotting factor activation cascade, is a serine
protease which not only catalyzes the conversion of fibrinogen into fibrin, but also clearly …

Human alpha-thrombin, the two (covalently linked)-chain, highly coagulant blood-clotting
enzyme was compared with its noncoagulant, yet estero/amidolytically active derivative …

Methodological problems encountered using chromogenic substrates on thrombin and Xa
are discussed:(1) influence of substrate on inhibitor;(2) influence of heparin;(3) optimal …