The preparation and properties of immobilised dipeptidyl-aminopeptidase I (cathepsin C)
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D W Hutchinson1, A Tunnicliffe
1Department of Chemistry, University of Warwick, Coventry, U.K.
Biochimica Et Biophysica Acta
|November 5, 1987
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.