Description
Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis.
Abbr
CPB1, Native (Porcine)
Applications
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 Creative Enzymes 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.
Product Overview
Protein determined by biuret.
Form
lyophilized powder. Contains HEPES buffer salts and carbohydrate
Enzyme Commission Number
EC 3.4.17.2
Unit Definition
One unit will hydrolyze 1.0 μmole of hippuryl-L-arginine per min at pH 7.65 at 25°C.
Synonyms
carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5
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