Two-step dissociation of bovine 6S procarboxypeptidase A by dimethylmaleylation
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference18 articles.
1. Reconstitution of bovine procarboxypeptidase A-S6 from the free subunits
2. Mode of activation and N-terminal sequence of subunit II in bovine procarboxypeptidase A and of porcine chymotrypsinogen C
3. On subunit II of bovine procarboxypeptidase A. enzymatic specificity after tryptic activation
4. Further characterization of subunit III of bovine procarboxypeptidase A-S6 as a non activatable zymogen
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1. Chymotrypsin C;Handbook of Proteolytic Enzymes;2013
2. How to Escape from Model Bias with a High-Resolution Native Data Set – Structure Determination of the PcpA-S6 Subunit III;Acta Crystallographica Section D Biological Crystallography;1996-03-01
3. Crystallographic Study of a Cleaved, Non/activatable Form of Porcine Zymogen E;Journal of Molecular Biology;1995-09
4. Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen E.;The EMBO Journal;1994-04
5. The activation peptide of pancreatic procarboxypeptidase a is the keystone of the bovine procarboxypeptidase A-S6 ternary complex;Biochemical and Biophysical Research Communications;1991-11
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