Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Antigenic Reactivity of Dephosphorylated αs1-Casein, Phosphopeptide from β-Casein and O-Phospho-L-serine towards the Antibody to Native αs1-Casein
Hajime OTANIHiroshi HORIAkiyoshi HOSONO
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1987 Volume 51 Issue 8 Pages 2049-2054

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Abstract

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.

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