THE ANTIGENIC COMPLEX OF STREPTOCOCCUS HÆMOLYTICUS

Author:

Lancefield Rebecca C.1

Affiliation:

1. From the Hospital of The Rockefeller Institute for Medical Research.

Abstract

The chemical and immunological characteristics of the type-specific substance (M) of Streptococcus hæmolyticus are considered. 1. A summary of the evidence for the protein nature of this substance follows: (a) It is precipiated by the usual protein precipitants such as, dilute alcohol, dilute acetic acid, and picric acid. (b) It contains 14 per cent protein nitrogen after considerable purification. (c) It is progressively destroyed by removal of the NH2 group by treatment with nitrous acid. (d) It is completely and readily digested by trypsin and by pepsin. 2. "Purified" extracts react in relatively high dilution with homologous antibacterial sera, but do not precipitate most heterologous antibacterial sera or sera potent in non-type-specific antibodies for the group reactive nucleoprotein P or for the species-specific probable carbohydrate C. Attempts to immunize rabbits with the type-specific protein have been unsuccessful, with simple salt solution extracts of streptococci as well as with purified solutions. This protein seems, therefore, to have the characteristics of a haptene. The type-specific substance (M) is contrasted with the so called nucleoprotein (P) which shows group relationships with nucleoproteins of related species and is the only fraction of hemolytic streptococcus extracts so far obtained which, after separation from the bacterial cell, is a true antigen leading to antibody production when injected into rabbits. The occurrence of another non-type-specific protein (Y) is suggested by occasional cross-reactions of purified M with certain antibacterial sera. Since it has not been separated from extracts containing the type-specific M, little is known of it either chemically or serologically. The cross-reaction disappears on tryptic or peptic digestion of the extract. The fact that such extracts do not show cross-reactions with anti-P sera is evidence that this non-type-specific protein is not P.

Publisher

Rockefeller University Press

Subject

Immunology,Immunology and Allergy

Cited by 82 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