天然和去折叠β-乳球蛋白的抗原性比较。

Comparison between the antigenicity of native and unfolded beta-lactoglobulin.

作者信息

Takahashi T, Yamauchi K, Kaminogawa S

机构信息

Department of Agricultural Chemistry, University of Tokyo, Japan.

出版信息

Agric Biol Chem. 1990 Mar;54(3):691-7.

PMID:1369986

Abstract

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.

摘要

通过酶联免疫吸附测定法（ELISA）检测β-乳球蛋白（β-LG）胰蛋白酶片段与小鼠抗β-LG抗血清的反应性，对β-乳球蛋白上的抗体结合位点（B细胞表位）进行了研究。四个肽片段（21位丝氨酸-40位精氨酸、41位缬氨酸-60位赖氨酸、102位酪氨酸-124位精氨酸和149位亮氨酸-162位异亮氨酸）与抗体结合。我们认为β-LG的B细胞表位包含在这些片段中。此外，这四个胰蛋白酶片段也与抗还原型羧甲基化β-LG抗血清发生反应。因此，β-LG分子的去折叠被认为不会影响β-LG上抗体结合位点的定位。