Specificity of antigenic recognition of antibody heavy chain

Author:

Abstract

The specificity of antigenic recognition of the component chains of purified dinitrophenyl and trinitrophenyl antibodies was examined. Heavy chains were rendered soluble at neutral pH, either by prior reaction of the parent antibodies with D,L-alanine N -carboxy anhydride, or by mixing heavy chain with light chain of non-specific IgG. The degree of homologous light chain contamination of these heavy chain preparations was found to be less than 2 %, either by immune precipitation, or by end-group analysis. Association constants of the heavy chains of both antibodies with several closely related haptenes were measured by fluorescence quenching. Heavy chains differentiated among these haptenes in the same manner as the parent antibodies, though considerable binding affinity was lost. When specific homologous light chains were added to the heavy chain preparations, association constants were increased, but without change in relative selectivity. Binding activity of light chains alone could not be measured. The heavy chain, then, appears to bear the specificity of its parent molecule. Whether or not homologous light chain contributes additional specific information with respect to antigenic recognition or simply plays a non-specific modulating role cannot be answered from these experiments.

Publisher

The Royal Society

Subject

General Medicine

Cited by 50 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3