Comparison between the Antigenicity of Native and Unfolded β-Lactoglobulin(Biological Chemistry)
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概要
- 論文の詳細を見る
The antibody binding sites (B-cell epitopes) on β-lactoglobulin (β-LG) were surveyed by assaying the reactivity of the tryptic fragments of β-LG to mouse anti-β-LG antiserum with ELISA. Four peptide fragments (the residues ^<21>Ser-^<40>Arg, ^<41>Val-^<60>Lys, ^<102>Tyr-^<124>Arg, and ^<149>Leu-^<162>Ile) bound the antibodies. We considered that B-cell epitopes of β-LG were included in these fragments. Furthermore, these four tryptic fragments were also reactive with the antiserum to RCM β-LG. Therefore, the unfolding of the β-LG molecule is considered not to influence the localization of the antibody binding sites on β-LG.
- 社団法人日本農芸化学会の論文
- 1990-03-23
著者
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TAKAHASHI Takeshi
Department of Electrical and Electronic Engineering, Akita University
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YAMAUCHI Kunio
Department of Agricultural Chemistry, The University of Tokyo
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KAMINOGAWA Shuichi
Department of Food Science and Technology, College of Bioresource Sciences, Nihon University
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Yamauchi Kunio
Department Of Agricultural Chemistry The University Of Tokyo
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Kaminogawa Shuichi
Department Of Agricultural Chemistry The University Of Tokyo
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Kaminogawa Shuichi
Department Of Agricultural Chemistry Faculty Of Engineering The University Of Tokyo
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Takahashi Takeshi
Department Of Agricultural Chemistry The University Of Tokyo
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