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.
Rapid Communication| April 01 1988
Proteolytic specificity of chicken cathepsin L on bovine β-casein
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Eric Dufour, Bruno Ribadeau-Dumas; Proteolytic specificity of chicken cathepsin L on bovine β-casein. Biosci Rep 1 April 1988; 8 (2): 185–191. doi: https://doi.org/10.1007/BF01116463
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