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, Recombinant (Rat)
Applications
Carboxypeptidase B (EC 3.4.17.2, protaminase, pancreatic carboxypeptidase B, tissue carboxypeptidase B, peptidyl-L-lysine [L-arginine]hydrolase) is a carboxypeptidase that preferentially acts upon basic amino acids, such as arginine and lysine. This serum enzyme is also responsible for rapidly metabolizing the C5a protein into C5a des-Arg, with one less amino acid.
Product Overview
Caspase 3 is synthesized as a 32 kDa proenzyme. The active enzyme is a heterodimer of two large (17 kDa) subunits and two small (12 kDa) subunits.
Form
Lyophilized from 20 mM Tris, pH 8.0 + 50 mM NaCl.
Enzyme Commission Number
EC 3.4.17.2
Activity
50-55 units/mg protein carboxypeptidase B
Pathway
Complement and Coagulation Cascades, organism-specific biosystem; Complement and coagulation cascades, conserved biosystem; Protein digestion and absorption, organism-specific biosystem
Function
carboxypeptidase activity; metallocarboxypeptidase activity; zinc ion binding
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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