Merck, C9584-1MG, Carboxypeptidase B from porcine pancreas

Application
Carboxypeptidase B has been used in a study to develop a non-invasive pregnancy assay for use in both captive and wild polar bears. Carboxypeptidase B has been used in a study that identified new potential biomarkers of acute pancreatitis.
The enzyme from Sigma has been used to develop homogeneous time-resolved fluorescence (HTRF) assay for measuring carboxypeptidase B activity in a miniaturized high-throughput screening format. It has been used to evaluate the impact of the C-terminal lysine(s) in human plasminogen binding to Bifidobacterium. The effect of treatment with carboxypeptidase B, which is a C-terminal lysine-specific endopeptidase, is measured using flow cytometry analysis.
Biochem/physiol Actions
Carboxypeptidase B is a proteolytic enzyme capable of rapidly hydrolyzing peptide bonds to release certain carboxyl-terminal basic amino acids from peptides and proteins. Its molecular mass is 34,300±600 Da. It contains one non-dialyzable gram atom of zinc per mole. The enzyme activity is inhibited by metal chelating agents 1, 10-phenanthroline, 8-hydroxyquinoline-5-sulfonic acid, and 2,2′-dipyridyl.
Packaging
Package size based on protein content
Physical form
Contains HEPES buffer salts, zinc chloride and carbohydrate
Preparation Note
Treated with protease inhibitor, AEBSF, to eliminate serine protease activity.
Analysis Note
Protein determined by biuret.
Other Notes
One unit will hydrolyze 1.0 μmole of hippuryl-L-arginine per min at pH 7.65 at 25 °C.