Carboxypeptidase B

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.

PMSF Treated:

• ≥70 units per mg protein
• PMSF treated to inhibit tryptic and chymotryptic activities.
• Solution in 100mM sodium chloride. 
• Chymotrypsin and trypsin are less than 0.02%.

Untreated:

• ≥170 units per mg protein
• Chromatographically purified.
• A solution in 100mM sodium chloride.
• Chymotrypsin and trypsin ≤ 0.02%.

Store at -20°C.

One Unit hydrolyzes one micromole of hippuryl-L-arginine per minute at 25°C, pH 7.65.

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