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C5233 Sigma

Carboxypeptidase B from human pancreas

50-55 units/mg protein carboxypeptidase B

Synonym: Peptidyl-L-Lysine[L-arginine] hydrolase

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Properties

Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Biochemicals and Reagents, Carboxypeptidase B, Enzyme Class Index,
InChI Key   TWURVFFNODFJBJ-UHFFFAOYSA-N
impurities   ≤0.2% chymotrypsin
  ≤0.2% trypsin
  ≤1 unit/mg protein carboxypeptidase A
shipped in   dry ice
storage temp.   −20°C
Gene Information   human ... CPB1(1360)

Description

Unit Definition

One unit will hydrolyze 1 μmole of hippuryl-L-arginine per minute at pH 7.7 at 25 °C

Physical form

Solution in 0.05 M NaOAc pH 5.0 + 1.0 M NaCl + 0.01% NaN3

Application

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.

Biochem/physiol Actions

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 34,000 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.

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Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
1
Protocols & Articles

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Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

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