Schröder S, Hoch W, Becker C M, Grenningloh G, Betz H
ZMBH, Universität Heidelberg, Federal Republic of Germany.
Biochemistry. 1991 Jan 8;30(1):42-7. doi: 10.1021/bi00215a007.
The inhibitory glycine receptor (GlyR) is a ligand-gated chloride channel protein that occurs in developmentally regulated isoforms in the vertebrate central nervous system. Monoclonal antibodies (mAbs) against the GlyR distinguish neonatal and adult GlyR proteins by identifying distinct alpha subunit variants within these receptor isoforms. Here, bacterially expressed fusion proteins of the rat GlyR alpha 1 subunit were used to localize the major antigenic epitopes of this protein within its N-terminal 105 amino acids. Synthetic peptides allowed further fine mapping of two mAb binding domains. MAb 2b, specific for the adult alpha 1 subunit, bound to a peptide corresponding to amino acids 1-10, whereas mAb 4a, which recognizes both neonatal and adult GlyR isoforms, reacted with a peptide representing residues 96-105 of the alpha 1 polypeptide. These data define unique and common antigenic epitopes on GlyR alpha subunit variants.
抑制性甘氨酸受体（GlyR）是一种配体门控氯离子通道蛋白，在脊椎动物中枢神经系统中以发育调控的亚型形式存在。针对GlyR的单克隆抗体（mAb）通过识别这些受体亚型内不同的α亚基变体来区分新生和成年GlyR蛋白。在此，大鼠GlyRα1亚基的细菌表达融合蛋白被用于在其N端105个氨基酸内定位该蛋白的主要抗原表位。合成肽允许对两个单克隆抗体结合域进行进一步的精细定位。对成年α1亚基特异的单克隆抗体2b与对应于氨基酸1-10的肽结合，而识别新生和成年GlyR亚型的单克隆抗体4a与代表α1多肽残基96-105的肽发生反应。这些数据定义了GlyRα亚基变体上独特和共同的抗原表位。
