Amino acid sequence of penicillopepsin. II. Isolation and characterization of thermolytic peptides
- 1 October 1976
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 54 (10) , 885-894
- https://doi.org/10.1139/o76-126
Abstract
The determination of the amino acid sequences of 70 peptides obtained from a thermolytic digest of penicillopepsin (EC 3.4.23.7) was described. Fifty-six unique sequences ranging from 2-13 amino acids were compiled. Among these was a heptapeptide whose sequence is nearly identical with that of the epoxide-reactive active site peptide of porcine pepsin (EC 3.4.23.1). Considering unrecognized overlaps, a minimum of 272 and a maximum of 293 unique amino acids have been obtained. They account for about 90% of the amino acids of the enzyme.This publication has 4 references indexed in Scilit:
- Amino acid sequence of penicillopepsin. I. Isolation and characterization of the chymotryptic peptidesCanadian Journal of Biochemistry, 1976
- Amino acid sequence of penicillopepsin. III. Isolation and characterization of amino terminal, tryptic, and tryptophanyl peptidesCanadian Journal of Biochemistry, 1976
- Amino acid sequence of penicillopepsin. IV. Myxobacter AL-1 protease II and Staphylococcus aureus protease fragments and homology with pig pepsin and chymosinCanadian Journal of Biochemistry, 1976
- Proteolytic enzymes of Penicillium janthinellumBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964