Antigenic Reactivity of Dephosphorylated αs1-Casein, Phosphopeptide from β-Casein and O-Phospho-L-serine towards the Antibody to Native αs1-Casein
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概要
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To study whether the phosphoserine residue is associated with the antigenicity of bovine αs1-casein, we examined the antigenic reactivity of dephosphorylated αs1-casein, peptide 1-25 from bovine β-casein and three chemical reagents with IgG antibody specific to native αs1-casein by an enzyme-linked immunosorbent assay. The reaction between native αs1-casein and its IgG antibody was inhibited more strongly by native αs1-casein than by dephosphorylated αs1-casein. Peptide 1-25, having a phosphoserine residue-concentrated region from bovine β-casein, noticeably inhibited the reaction between native αs1-casein and its antibody. Furthermore, the O-phospho-L-serine residue inhibited the reaction of peptide 61-123 with anti-native αs1-casein antibody, although L-serine and sodium phosphate showed no measurable inhibition. These results suggest that the phosphoserine residue associated with part of an antigenic site in bovine αs1-casein.
- 社団法人 日本農芸化学会の論文
著者
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Hosono Akiyoshi
Department Of Animal Husbandry Faculty Of Agriculture Shinsyu University
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Otani Hajime
Department Of Crop And Animal Science Faculty Of Agriculture Shinshu University
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HORI Hiroshi
Department of Agricultural Chemistry, Faculty of Agriculture, Tamagawa University
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HOSONO Akiyoshi
Department of Zoo technical Science, Faculty of Agriculture, Shinshu University
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