Inactivation of pepsin by diphenyldiazomethane.
- 1 October 1965
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 54 (4) , 1161-1167
- https://doi.org/10.1073/pnas.54.4.1161
Abstract
Diphenyldiazomethane (DDM) rapidly inactivates crystalline swine pepsin at pH 5, as measured by its enzymic activity toward hemoglobin and acetyl-L-phenylalanyl-L-tyrosine. With C14-labeled DDM, radioactivity is incorporated into the protein, presumably by esterifica-tion of reactive carboxyl groups. Treatment of pepsinogen with labeled DDM causes an inhibition of its potential enzymic activity, with incorporation of C14 into the protein.This publication has 15 references indexed in Scilit:
- Specific and Reversible Inactivation of PepsinJournal of Biological Chemistry, 1965
- Structural Studies of Ribonuclease. XVII. A Reactive Carboxyl Group in Ribonuclease*Biochemistry, 1965
- Spectrophotometric Determination of the Kinetics of the Pepsin-Catalyzed Hydrolysis of Certain Dipeptide SubstratesJournal of the American Chemical Society, 1965
- Poly-α-amino-acids containing L-Glutamyl Residues as Substrates for PepsinNature, 1962
- CHEMICAL DERIVATIVES OF ALPHA-CHYMOTRYPSINOGEN .4. COMPARISON OF REACTIONS OF ALPHA-CHYMOTRYPSINOGEN AND OF SIMPLE CARBOXYLIC ACIDS WITH DIAZOACETAMIDE1961
- STUDIES ON BEEF SPLEEN CATHEPSIN AProceedings of the National Academy of Sciences, 1960
- Pepsin-catalysed transpeptidation of the amino-transfer typeBiochemical Journal, 1959
- Studies on the amide and C-terminal residues in proteins. 2. The ammonia nitrogen and amide nitrogen of various native protein preparationsBiochemical Journal, 1958
- PEPTIDES OBTAINED BY PEPTIC HYDROLYSIS OF PERFORMIC ACID-OXIDIZED RIBONUCLEASEJournal of Biological Chemistry, 1956
- The active groups of pepsinJournal of Cellular and Comparative Physiology, 1956