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  • Title: The preparation and properties of immobilised dipeptidyl-aminopeptidase I (cathepsin C).
    Author: Hutchinson DW, Tunnicliffe A.
    Journal: Biochim Biophys Acta; 1987 Nov 05; 916(1):1-4. PubMed ID: 3663681.
    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.
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