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Carboxypeptidase A

Known as: Carboxypeptidases A, Carboxypeptidases A [Chemical/Ingredient] 
Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little… Expand
National Institutes of Health

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Highly Cited
1991
Highly Cited
1991
A novel plasminogen-binding protein has been isolated from human plasma utilizing plasminogen-Sepharose affinity chromatography… Expand
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Highly Cited
1989
Highly Cited
1989
Mast cell carboxypeptidase A has been isolated from the secretory granules of mouse peritoneal connective tissue mast cells (CTMC… Expand
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Highly Cited
1986
Highly Cited
1986
Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the… Expand
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Highly Cited
1986
Highly Cited
1986
A high-resolution x-ray crystallographic investigation of the complex between carboxypeptidase A (CPA; peptidyl-L-amino-acid… Expand
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Highly Cited
1985
Highly Cited
1985
The use of fluoro ketones as inhibitors of hydrolytic enzymes has been investigated. The acetylcholine analogues 6,6-dimethyl-1,1… Expand
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Highly Cited
1983
Highly Cited
1983
The crystal structure of bovine carboxypeptidase A (Cox) has been refined at 1.54 A resolution using the restrained least-squares… Expand
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Highly Cited
1980
Highly Cited
1980
The recently developed protein A-gold technique for the detection of intracellular antigenic sites on thin sections was utilized… Expand
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Highly Cited
1975
Highly Cited
1975
Abstract An endogenous morphine-like substance (MLF) found in rat and calf brains has a regional distribution correlating with… Expand
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Highly Cited
1972
Highly Cited
1972
  • R. Ambler
  • Methods in enzymology
  • 1972
  • Corpus ID: 26598253
Publisher Summary Carboxypeptidases are enzymes that remove amino acids one residue at a time from the C-termini of polypeptide… Expand
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Review
1971
Review
1971
Publisher Summary This chapter discusses the relationship of the three-dimensional structures of bovine carboxypeptidase A (CPA… Expand
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