Comparison between the antigenicity of native and unfolded beta-lactoglobulin.
The antibody binding sites (B-cell epitopes) on beta-lactoglobulin (beta-LG) were surveyed by assaying the reactivity of the tryptic fragments of beta-LG to mouse anti-beta-LG antiserum with ELISA. Four peptide fragments (the residues 21Ser-40Arg, 41Val-60Lys, 102Tyr-124 Arg, and 149Leu-162Ile) bound the antibodies. We considered that B-cell epitopes of beta-LG were included in these fragments. Furthermore, these four tryptic fragments were also reactive with the antiserum to RCM beta-LG. Therefore, the unfolding of the beta-LG molecule is considered not to influence the localization of the antibody binding sites on beta-LG.
Takahashi
T
T
Department of Agricultural Chemistry, University of Tokyo, Japan.
Yamauchi
K
K
Kaminogawa
S
S
D000595:Amino Acid Sequence; D000818:Animals; D000936:Antigen-Antibody Complex; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000032:analysis*; D005260:Female; D007106:Immune Sera; D007782:Lactoglobulins / Q000276:immunology* / Q000302:isolation & purification; D008892:Milk; D008958:Models, Molecular; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D011489:Protein Denaturation; D014357:Trypsin
D000936:Antigen-Antibody Complex; D000939:Epitopes; D007106:Immune Sera; D007782:Lactoglobulins; D010446:Peptide Fragments; D014357:Trypsin