title: The preparation and properties of immobilised dipeptidyl-aminopeptidase I (cathepsin C).
abstract: Dipeptidyl-aminopeptidase I (dipeptidyl-peptide hydrolase, EC 3.4.14.1) from bovine spleen has been immobilized by hydrophobic bonding to alkyl- or aryl-Sepharoses. Optimum binding occurred with octyl- and phenyl-Sepharoses. The activity of the immobilised dipeptidyl-aminopeptidase I has been determined using glycylarginyl-p-nitroanilide as substrate and the pH optimum of the immobilised enzyme determined as well as the stability of the enzyme to repeated use. Preliminary studies using immobilised dipeptidyl-aminopeptidase I for the digestion of methionine enkephalin have been carried out using reverse-phase HPLC to analyse the reaction.
authors: Department of Chemistry, University of Warwick, Coventry, U.K.
authors: D W
authors: DW
authors: Hutchinson
authors: A
authors: A
authors: Tunnicliffe
mesh_terms: D000818:Animals; D020789:Cathepsin C; D002417:Cattle; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D013154:Spleen / Q000201:enzymology
chemical_list: D004800:Enzymes, Immobilized; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D020789:Cathepsin C