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Carboxypeptidase B

Known as: Carboxypeptidase B [Chemical/Ingredient], Protaminase 
A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. The enzyme catalyzes the preferential cleavage of a C-terminal peptidyl-L… Expand
National Institutes of Health

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Related topics

9 relations
CPB1 geneIn BloodProcess of secretionantagonists & inhibitors
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Procarboxypeptidase B

Papers overview

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Highly Cited
2009
Highly Cited
2009
Regulation of Chemerin Bioactivity by Plasma Carboxypeptidase N, Carboxypeptidase B (Activated Thrombin-activable Fibrinolysis Inhibitor), and Platelets*
Chemerin is a potent chemoattractant for cells expressing the serpentine receptor CMKLR1 (chemokine-like receptor 1), such as… Expand
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Highly Cited
1997
Highly Cited
1997
On the Mechanism of the Antifibrinolytic Activity of Plasma Carboxypeptidase B*
The precursor of plasma carboxypeptidase B (pCPB) also known as thrombin-activable fibrinolysis inhibitor can be converted by… Expand
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Highly Cited
1996
Highly Cited
1996
TAFI, or Plasma Procarboxypeptidase B, Couples the Coagulation and Fibrinolytic Cascades through the Thrombin-Thrombomodulin Complex*
TAFI (thrombin-activatable fibrinolysis inhibitor) is a recently discovered plasma protein that can be activated by thrombin… Expand
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Highly Cited
1996
Highly Cited
1996
Carboxypeptidase E Activity Is Deficient in Mice with the fat Mutation
Carboxypeptidase E (CPE) is involved in the biosynthesis of many peptide hormones and neurotransmitters. Mice with the fat… Expand
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Highly Cited
1995
Highly Cited
1995
Purification and Characterization of TAFI, a Thrombin-activable Fibrinolysis Inhibitor (*)
Previous studies demonstrated that tissue plasminogen activator-induced fibrinolysis in vitro is retarded in the presence of… Expand
Highly Cited
1991
Highly Cited
1991
Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma.
A novel plasminogen-binding protein has been isolated from human plasma utilizing plasminogen-Sepharose affinity chromatography… Expand
Review
1988
Review
1988
Basic carboxypeptidases: regulators of peptide hormone activity.
  • R. Skidgel
  • Trends in pharmacological sciences
  • 1988
    • Corpus ID: 4265194
Abstract The importance of basic carboxypeptidases (i.e. enzymes that cleave C-terminal arginine or lysine from proteins or… Expand
Highly Cited
1987
Highly Cited
1987
Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and α-factor precursor processing
The yeast KEX1 gene product has homology to yeast carboxypeptidase Y. A mutant replacing serine at the putative active site of… Expand
Highly Cited
1984
Highly Cited
1984
Carboxypeptidase B-like converting enzyme activity in secretory granules of rat pituitary.
  • V. Hook, Y. Loh
  • Proceedings of the National Academy of Sciences…
  • 1984
    • Corpus ID: 30525475
Recent amino acid sequence data suggest that trypsin-like and carboxypeptidase B-like activities are required for the processing… Expand
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Highly Cited
1979
Highly Cited
1979
Design of potent and specific inhibitors of carboxypeptidases A and B.
The combination in one molecule of functional groups that can interact specifically with different substrate binding areas at the… Expand
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