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.
Note carboxypeptidase product code COBPMS has been discontinued and superseded by product code COBC listed below.
Carboxypeptidase Y (COY)
Chymotrypsin, TLCK-treated (CDTLCK)
Clostripain, Endo-Arg-C (CP)
Protease, Stap, Endo-Glu-C (STAP)
Trypsin, SeqENZ (TRSEQII) & Modified (TRSEQZ)
One Unit hydrolyzes one micromole of hippuryl-L-arginine per minute at 25°C, pH 7.65.
Carboxypeptidase B Products
Chromatographically purified. A solution in 100mM sodium chloride. Chymotrypsin and trypsin 0.02%.
Store at -20°C.
Ice Pack required
≥170 units per mg protein