Carboxypeptidase B from porcine pancreas, CAS No.9025-24-5
Synonyms
DTXSID801009277 | FT-0623486 | Carboxypeptidase B from human pancreas, 50-55 units/mg protein carboxypeptidase B | 4-[[1-[[1-[2-[(1-benzylsulfanyl-1-oxo-3-phenylpropan-2-yl)carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobu
Grade
EnzymoPure™
Product Description
Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and ornithine from the C-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 7.9, and the pI is 6.0. Carboxypeptidase B is competitively inhibited by arginine, lysine and ornithine. The enzyme is not inhibited by di-isopropylfluorophosphate (DFP), but it is inhibited by metal chelating agents, e.g., 1,10-phenanthroline. 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.
Specifications & Purity
EnzymoPure™, ≥170 units/mg protein
Biochemical and Physiological Mechanisms
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 zin
This compound belongs to the class of organic compounds known as oligopeptides. These are organic compounds containing a sequence of between three and ten alpha-amino acids joined by peptide bonds.
External Descriptors
Not available
1. Djoumbou Feunang Y, Eisner R, Knox C, Chepelev L, Hastings J, Owen G, Fahy E, Steinbeck C, Subramanian S, Bolton E, Greiner R, and Wishart DS. ClassyFire: Automated Chemical Classification With A Comprehensive, Computable Taxonomy. Journal of Cheminformatics, 2016, 8:61.
K1928130