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Proteolytic specificity of chicken cathepsin L on bovineβ-casein (1988)

Dufour, Eric ; Ribadeau-Dumas, Bruno

Springer

Bioscience reports 8 (1988), S. 185-191

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ISSN: 1573-4935

Keywords: cathepsin L ; specificity ; β-casein ; proteolysis

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology

Notes: 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01116463

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