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抗人肌红蛋白单克隆抗体的抗原特异性

Antigenic specificity of monoclonal antibodies to human myoglobin.

作者信息

East I J, Hurrell J G, Todd P E, Leach S J

出版信息

J Biol Chem. 1982 Mar 25;257(6):3199-202.

PMID:6174517
Abstract

Two monoclonal antibodies directed against different sites of the human myoglobin molecule have been tested for their cross-reactivities against several myoglobins including seven from mammalian species. The relation between their cross-reactivities and their amino acid sequences had led to a possible localization of two antigenic domains in human myoglobin. Each domain includes residues previously considered not to be directly involved in the antigenic structure of myoglobin. Unlike polyclonal serum antibodies, monoclonal hybridoma antibodies directed to a native protein often fail to bind to supposedly antigenic protein fragments. This is explicable in terms of the concept of antigenic domains. Such domains are numerous and overlapping, each comprising a number of contributory amino acid side chains which need not necessarily include continuous sequences of amino acids and which need not exhibit measurable antigenicity in isolation from the rest of the domain.

摘要

针对人肌红蛋白分子不同位点的两种单克隆抗体,已针对几种肌红蛋白进行了交叉反应性测试,其中包括来自哺乳动物物种的七种肌红蛋白。它们的交叉反应性与其氨基酸序列之间的关系,已使人肌红蛋白中两个抗原结构域的可能定位成为可能。每个结构域都包含先前被认为不直接参与肌红蛋白抗原结构的残基。与多克隆血清抗体不同,针对天然蛋白质的单克隆杂交瘤抗体通常无法与假定的抗原性蛋白质片段结合。根据抗原结构域的概念,这是可以解释的。此类结构域数量众多且相互重叠,每个结构域都包含许多起作用的氨基酸侧链,这些侧链不一定包括连续的氨基酸序列,并且在与结构域的其余部分分离时不一定表现出可测量的抗原性。

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