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

Technical Report · Mon Jan 01 00:00:00 EST 1979

DOI:https://doi.org/10.2172/5734455· OSTI ID:5734455

DeTraglia, M. C.

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.

• Research Organization: Rochester Univ., NY (USA). Dept. of Radiation Biology and Biophysics
• DOE Contract Number: EY-76-C-02-3490
• OSTI ID: 5734455
• Report Number(s): UR-3490-1689
• Resource Relation: Other Information: Thesis
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PROTEINS
TRYPTOPHAN
TRYPSIN
LABELLING
AMINO ACIDS
ENZYMES
PH VALUE
PHOTOLYSIS
REAGENTS
SCINTISCANNING
TRACER TECHNIQUES
AZOLES
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
COUNTING TECHNIQUES
DECOMPOSITION
DIAGNOSTIC TECHNIQUES
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HYDROLASES
INDOLES
ISOTOPE APPLICATIONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PEPTIDE HYDROLASES
PHOTOCHEMICAL REACTIONS
PYRROLES
RADIOISOTOPE SCANNING
550201* - Biochemistry- Tracer Techniques