CARBOXYPEPTIDASE B Chemical Properties

storage temp. 

-20°C

solubility 

water: 1 mg/mL

form 

powder

color 

white

biological source

Porcine pancreas

Water Solubility 

water: 1mg/mL

Specific Activity

50-55units/mg protein carboxypeptidase B

InChIKey

TWURVFFNODFJBJ-UHFFFAOYSA-N

SMILES

C(O)(=O)CCC(NC(C)C(NC(C)C(N1CCCC1C(=O)NC(CC1=CC=CC=C1)C(SCC1=CC=CC=C1)=O)=O)=O)=O

Safety Information

Hazard Codes 

Xi,B,Xn

Risk Statements 

36-42-36/37/38

Safety Statements 

26-36-36/37-24-22

WGK Germany 

3

Storage Class

10 - Combustible liquids

Hazard Classifications

Eye Irrit. 2
Resp. Sens. 1
Skin Irrit. 2
STOT SE 3

MSDS

• Language:English Provider:SigmaAldrich

CARBOXYPEPTIDASE B Usage And Synthesis

Uses

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.

Uses

Carboxypeptidase B from Sigma has been used as a reference for assaying carboxypeptidase activity in lysed pituitary granules derived from the anterior and intermediate lobes of rat. The enzyme has also been used to digest plasma samples by removing C-terminal basic amino acids, to get a distinct band for each allotype during C4 electrophoresis.

General Description

Native carboxypeptidase B catalyzes the release of C-terminal from basic amino acids, arginine, lysine, or ornithine from polypeptides. Inhibited by EDTA and other Zn²⁺ chelators.

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.

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