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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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Highly Cited
2009
Highly Cited
2009
Chemerin is a potent chemoattractant for cells expressing the serpentine receptor CMKLR1 (chemokine-like receptor 1), such as… Expand
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Review
2008
Review
2008
Thrombin-activatable procarboxypeptidase B (proCPB or thrombin-activatable fibrinolysis inhibitor or TAFI) is a plasma… Expand
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Highly Cited
2007
Highly Cited
2007
ABSTRACT Anopheles gambiae is the major African vector of Plasmodium falciparum, the most deadly species of human malaria… Expand
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Highly Cited
1998
Highly Cited
1998
Using synthetic substrates we have characterised carboxypeptidase activity in gut extracts from Helicoverpa armigera larvae… Expand
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Highly Cited
1997
Highly Cited
1997
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 (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 (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
Previous studies demonstrated that tissue plasminogen activator-induced fibrinolysis in vitro is retarded in the presence of… Expand
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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
1984
Highly Cited
1984
  • V. Hook, Y. P. 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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