CARBOXYPEPTIDASEA FROM BOVINE PANCREAS

Description_x000D_ General description_x000D_ Carboxypeptidase A (CPA) is a secreted protease is liberated after the activation of mast cells to facilitate acute anaphylaxis. Carboxypeptidase A has a long half-life in vivo, when compared to other secreted proteases._x000D_ Application_x000D_ Carboxypeptidase A from bovine pancreas has been used in in vitro simulated digestion._x000D_ Carboxypeptidase A from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase A in Escherichia coli. Carboxypeptidase A from bovine pancreas has also been used in a study to investigate the isolation and partial characterization of precursor forms of ostrich carboxypeptidase._x000D_ Packaging_x000D_ 500, 2500, 5000 units in glass bottle_x000D_ Biochem/physiol Actions_x000D_ 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.†_x000D_ Unit Definition_x000D_ One unit will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 at 25 °C._x000D_ Preparation Note_x000D_ Treated with phenylmethylsulfonyl fluoride to eliminate trypsin and chymotrypsin activity. Dialyzed and recrystallized: aqueous suspension with toluene added._x000D_ Analysis Note_x000D_ Protein determined by E1%/278