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Isolation of an active peptide fragment from human serum albumin and its synergism with α‐tocopherol
Author(s) -
Hatate Hideo
Publication year - 1998
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-998-0302-6
Subject(s) - tetrapeptide , peptide , chemistry , human serum albumin , bovine serum albumin , biochemistry , hydrolysate , amino acid , peptide sequence , linoleic acid , chromatography , serum albumin , hydrolysis , fatty acid , gene
An active peptide was isolated from hydrolysates of human serum albumin. This peptide was initially isolated by gel permeation chromatography and subsequent reversed‐phase high‐performance liquid chromatography. This active peptide, composed of 10 amino acid residues, was further hydrolyzed with a lysyl endopeptidase to give two peptide fragments. Only one fragment, identified as the tetrapeptide Leu‐Gln‐His‐Lys, was found to have activity comparable to the original peptide and corresponded to the amino acid residues 103–106 of human serum albumin. Among these four amino acid residues, the His‐Lys sequence seemed to be important in the occurrence of potent activity by comparison of the structural similarity with another active tetrapeptide, Asp‐Thr‐His‐Lys, which had been previously isolated from bovine serum albumin hydrolysates. In addition, the active fragment showed potent synergism by preventing consumption of α‐tocopherol during the autoxidation of linoleic acid.