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.

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