Comparison of the Proteolytic Specificities of Bovine and Porcine Pepsin A.
- 1 January 1977
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 31b (2) , 149-156
- https://doi.org/10.3891/acta.chem.scand.31b-0149
Abstract
Bovine pepsin A [EC 3.4.23.1] inactivates pancreatic RNase through a limited proteolysis the same way as does porcine pepsin A. The specific activity is lower and more dependent on the ionic strength. The proteolytic specificity of bovine pepsin A was investigated with B-chain of oxidized porcine insulin as the substrate. The specificity resembles qualitatively that of porcine pepsin but with quantitative differences.This publication has 4 references indexed in Scilit:
- Studies on the Specificity of Pepsin*Biochemistry, 1967
- THE AMINO ACID SEQUENCE OF PSEUDOMONAS CYTOCHROME C-551Biochemical Journal, 1963
- THE LIMITED DIGESTION OF RIBONUCLEASE WITH PEPSINJournal of Biological Chemistry, 1956
- The amino-acid sequence in the phenylalanyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysatesBiochemical Journal, 1951