Carboxypeptidase B from human pancreas, 50-55 units/mg protein carboxypeptidase B

Stock Code: 3579222
Manufacturer Part No: C5233-100UG
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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


Mutations in the carboxypeptidase B (CPB1) gene is implicated with increased susceptibility to pancreatic cancer development and progression. Elevated levels of CPB1 is associated with low grade breast tumors and lymph node positive grade 1 tumors.


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.


General description


Carboxypeptidase B is mapped to human chromosome 3q24. Carboxypeptidase B belongs to A/B subfamily of carboxypeptidases.


Physical form


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


Unit Definition


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

Quality Level200
InChI keyTWURVFFNODFJBJ-UHFFFAOYSA-N
InChI1S/C31H38N4O7S/c1-20(32-26(36)15-16-27(37)38)28(39)33-21(2)30(41)35-17-9-14-25(35)29(40)34-24(18-22-10-5-3-6-11-22)31(42)43-19-23-12-7-4-8-13-23/h3-8,10-13,20-
ManufacturerSIGMA-ALDRICH
Impurities≤1 unit/mg protein carboxypeptidase A, ≤0.2% chymotrypsin, ≤0.2% trypsin
Formsolution

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