Work

I. Use of m- and p-azidobenzamidines, 4-fluoro-3-nitro-phenylazide, and 3-azido-1,2,4-triazole as photoaffinity probes of tryptic binding site conformation. II. Analysis of tryptophan in proteins by an acidic reaction of 3-diazonium-1,2,4-triazole

Year: 1979

Type: report

Abstract: Meta- and para-azidobenzamidine have been prepared and evaluated as photoaffinity labels. The compounds inhibit trypsin reversibly in the dark and are competitive with substrate binding. Upon photolysis, irreversible noncompetitive inhibition is observed and is dependent upon concentration, photolysis time, and pH. Specificity of the probes is indicated by experiments in which p-tosyl-L-arginine methyl ester, a trypsin substrate, is used to protect against photoinactivation.

Source: OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information)

DOI: 10.2172/5734455

Author: M.C. DeTraglia

Language: English

Topic: Protease and Inhibitor Mechanisms

Subfield: Cancer Research

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W331128002

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