Biochem/physiol Actions

CarboxypeptidaseA is attached covalently to agarose or aldehyde and is effective for immobilization studies.

Carboxypeptidase as isolated from bovine pancreas glands is a metalloenzyme that contains 1 g atom of zinc per mole of protein. It catalyzes the hydrolysis of the carboxyl-terminal peptide bond in peptides and proteins. It is primarily specific to aromatic and hydrophobic side chains such as phenylalanine, tryptophan or leucine. The enzyme also exhibits esterase activity. It is inhibited by β-phenylpropionate and indole acetate.

General description

Carboxypeptidase A-agarose product is prepared by the immobilization of carboxypeptidase A, originally isolated from the bovine pancreas, to activated 4% crosslinked beaded agarose.

Physical form

Suspension in 2.0 M (NH₄)₂SO₄, pH 7

Unit Definition

One unit will hydrolyze 1.0 µmole of hippuryl-L-phenylalanine per min at pH 7.5 at 25 °C.