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Proteolytic specificity of chicken cathepsin L on bovineβ-casein

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Bioscience Reports

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 P ′1 . Looking at the amino acid residues on the amino side of the scissile bond we found three times the Tyr-Pro pair at P ′1 –P ′2 positions and that the S ′1 subsite can interact with modified amino acids such as phosphoserine.

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Abbreviations

RP-HPLC:

reverse phase high performance liquid chromatography

NMec:

N-methyl coumarylamide

TEA:

triethylamine

TFA:

trifluoroacetic acid

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Authors and Affiliations

  1. S.R.V., I.N.R.A. de Theix, 63122, Ceyrat, France

    Eric Dufour

  2. I.N.R.A., Jouy en Josas, 78350, Jouy en Josas, France

    Bruno Ribadeau-Dumas

Authors
  1. Eric Dufour
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  2. Bruno Ribadeau-Dumas
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Dufour, E., Ribadeau-Dumas, B. Proteolytic specificity of chicken cathepsin L on bovineβ-casein. Biosci Rep 8, 185–191 (1988). https://doi.org/10.1007/BF01116463

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  • DOI: https://doi.org/10.1007/BF01116463

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