title: Proteolytic specificity of chicken cathepsin L on bovine beta-casein.
abstract: The proteolytic specificity of chicken cathepsin L was studied using bovine beta-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.
authors.affiliation: S.R.V., I.N.R.A. de Theix, Ceyrat, France.
authors.forename: E
authors.initials: E
authors.lastname: Dufour
authors.forename: B
authors.initials: B
authors.lastname: Ribadeau-Dumas
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002364:Caseins / Q000378:metabolism*; D056668:Cathepsin L; D002403:Cathepsins / Q000378:metabolism*; D002417:Cattle; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D003546:Cysteine Endopeptidases; D010450:Endopeptidases; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D002364:Caseins; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L