2. Academic Validation
  3. The preparation and properties of immobilised dipeptidyl-aminopeptidase I (cathepsin C)

The preparation and properties of immobilised dipeptidyl-aminopeptidase I (cathepsin C)

  • Biochim Biophys Acta. 1987 Nov 5;916(1):1-4. doi: 10.1016/0167-4838(87)90203-2.
D W Hutchinson 1,  A Tunnicliffe
Affiliations

Affiliation

  • 1 Department of Chemistry, University of Warwick, Coventry, U.K.
PMID: 3663681 DOI: 10.1016/0167-4838(87)90203-2
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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