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Isolation and characterization of cytotoxic small peptides, α‐casecidins, from bovine αs1‐casein digested with bovine trypsin
Author(s) -
OTANI Hajime,
SUZUKI Hiroyuki
Publication year - 2003
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1046/j.1344-3941.2003.00135.x
Subject(s) - trypsin , cytotoxicity , bovine serum albumin , casein , chemistry , biochemistry , lysine , cytotoxic t cell , microbiology and biotechnology , amino acid , peptide , biology , in vitro , enzyme
Cytotoxic peptides were isolated from a trypsin digest of bovine αs1‐casein by a combination of ion‐exchange column chromatography and reversed‐phase high‐performance liquid chromatography as an indicator of cytotoxicity toward mouse spleen cells. Amino acids of the isolated peptides were sequenced as arginyl‐proly‐lysine, leucyl‐lysyl‐lysine and tyrosyl‐lysine, being compatible with sequences 1–3, 101–103 and 104–105 of bovine αs1‐casein, respectively. The isolated peptides displayed cytotoxicity toward healthy mouse T and B cells and human leukemic T and B cell lines in a commercially available serum‐free medium for lymphocytes, Celgrosser‐P, and were named α‐casecidins. Similar cytotoxicity was confirmed in chemically synthesized peptides corresponding to sequences 1–3, 101–103 and 100–105 of bovine αs1‐casein. The cytotoxicity induced by α‐casecidins was concluded to be because of necrosis, and was diminished in the presence of bovine serum albumin.