Proteolytic specificity of chicken cathepsin L on bovine β-casein. Issue 2 (April 1988)

• Record Type: Journal Article
• Authors: Dufour, Eric; Ribadeau-Dumas, Bruno
• Is Part Of: Bioscience reports. Volume 8:Issue 2(1988)
• Page Start: 185
• Page End: 191
• Publication Date: 1988-04
• Subjects: cathepsin L -- specificity -- β-casein -- proteolysis; Molecular biology -- Periodicals; Cytology -- Periodicals; 572.8
• DOI: 10.1007/BF01116463
• Languages: English
• ISSNs: 0144-8463

Abstract

Abstract : The proteolytic specificity of chicken cathepsin L was studied using bovine β-casein as substrate. The peptide mixtures obtained after various times of hydrolysis were separated by RP-HPLC and ten peptides were identified. Chicken cathepsin L accepts proline residues in all positions except P1 ′ . Looking at the amino acid residues on the amino side of the scissile bond we found three times the Tyr-Pro pair at P1 ′ –P2 ′ positions and that the S1 ′ subsite can interact with modified amino acids such as phosphoserine.