Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1963 Jan;49(1):109–116. doi: 10.1073/pnas.49.1.109

CARBOXYPEPTIDASE A: APPROACHES TO THE CHEMICAL NATURE OF THE ACTIVE CENTER AND THE MECHANISMS OF ACTION*

Bert L Vallee 1,2, James F Riordan 1,2,†, Joseph E Coleman 1,2,†
PMCID: PMC300637  PMID: 13995911

Full text

PDF
109

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. COLEMAN J. E., VALLEE B. L. Apocarboxypeptidase-substrate complexes. J Biol Chem. 1962 Nov;237:3430–3436. [PubMed] [Google Scholar]
  2. COLEMAN J. E., VALLEE B. L. Metallocarboxypeptidases. J Biol Chem. 1960 Feb;235:390–395. [PubMed] [Google Scholar]
  3. COLEMAN J. E., VALLEE B. L. Metallocarboxypeptidases: stability constants and enzymatic characteristics. J Biol Chem. 1961 Aug;236:2244–2249. [PubMed] [Google Scholar]
  4. COLEMAN J. E., VALLEE B. L. Metallocarboxypeptidasesubstrate complexes. Biochemistry. 1962 Nov;1:1083–1092. doi: 10.1021/bi00912a019. [DOI] [PubMed] [Google Scholar]
  5. FELBER J. P., COOMBS T. L., VALLEE B. L. The mechanism of inhibition of carboxypeptidase A by 1,10-phenanthroline. Biochemistry. 1962 Mar;1:231–238. doi: 10.1021/bi00908a006. [DOI] [PubMed] [Google Scholar]
  6. SANGER F. The terminal peptides of insulin. Biochem J. 1949;45(5):563–574. doi: 10.1042/bj0450563. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. WALSH K. A., SAMPATH KUMAR K. S., BARGETZI J. P., NEURATH H. Approaches to the selective chemical labeling of the active site of carboxypepticase A. Proc Natl Acad Sci U S A. 1962 Aug;48:1443–1449. doi: 10.1073/pnas.48.8.1443. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES