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

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Description

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.

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Pages: 142

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DeTraglia, M.C. January 1, 1979.

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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.

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Pages: 142

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Dep. NTIS, PC A07/MF A01.

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  • Report No.: UR-3490-1689
  • Grant Number: EY-76-C-02-3490
  • DOI: 10.2172/5734455 | External Link
  • Office of Scientific & Technical Information Report Number: 5734455
  • Archival Resource Key: ark:/67531/metadc1093141

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  • January 1, 1979

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DeTraglia, M.C. 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, report, January 1, 1979; United States. (digital.library.unt.edu/ark:/67531/metadc1093141/: accessed July 15, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.