• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

用羟基磷灰石柱色谱法从1、3、6、12和17型化脓性链球菌的酸提取物中纯化的M蛋白的特性。

The characteristics of M proteins purified by column chromatography with hydroxyapatite from acid extracts of Streptococcus pyogenes of types 1, 3, 6, 12 and 17.

作者信息

Vosti K L

出版信息

J Med Microbiol. 1978 Nov;11(4):453-62. doi: 10.1099/00222615-11-4-453.

DOI:10.1099/00222615-11-4-453
PMID:364064
Abstract

Purified M proteins were recovered from acid extracts of Streptococcus pyogenes, M-types 1, 3, 6, 12 and 17, by elution from columns of hydroxyapatite of the proteins precipitated with ammonium sulphate. M protein free from non-type-specific antigens was recovered only from M-type 12. Although similar fractions were not recovered from M-types 1, 3, 6 and 17, purified preparations containing a single cross-reactive antigen were obtained. In addition to the M proteins associated with cross-reactive antigens, type-specific antigens that did not stimulate opsonic antibodies were isolated from revealed molecular weights that ranged from 32,000 to 63,000 daltons, total amino acid compositions that were similar, and N-terminal amino acids that were variable.

摘要

从化脓性链球菌M1、M3、M6、M12和M17型的酸提取物中,通过从用硫酸铵沉淀的蛋白质的羟基磷灰石柱上洗脱,回收纯化的M蛋白。仅从M12型中回收了不含非型特异性抗原的M蛋白。虽然从M1、M3、M6和M17型中未回收类似的组分,但获得了含有单一交叉反应抗原的纯化制剂。除了与交叉反应抗原相关的M蛋白外,还从揭示的分子量范围为32,000至63,000道尔顿、总氨基酸组成相似且N端氨基酸可变的物质中分离出不刺激调理素抗体的型特异性抗原。

相似文献

1
The characteristics of M proteins purified by column chromatography with hydroxyapatite from acid extracts of Streptococcus pyogenes of types 1, 3, 6, 12 and 17.用羟基磷灰石柱色谱法从1、3、6、12和17型化脓性链球菌的酸提取物中纯化的M蛋白的特性。
J Med Microbiol. 1978 Nov;11(4):453-62. doi: 10.1099/00222615-11-4-453.
2
M protein of type 12 Strepto coccus pyogenes. Isolation by electrofocusing and some molecular weight-dependent properties.12型化脓性链球菌的M蛋白。通过等电聚焦进行分离及一些分子量依赖性特性
Pathol Microbiol (Basel). 1975;42(3):147-58.
3
Human immune response to immunization with a structurally defined polypeptide fragment of streptococcal M protein.人类对用链球菌M蛋白的结构明确的多肽片段进行免疫接种的免疫反应。
J Exp Med. 1979 Oct 1;150(4):862-77. doi: 10.1084/jem.150.4.862.
4
Recombinant tetravalent group A streptococcal M protein vaccine.重组A群链球菌M蛋白四价疫苗
J Immunol. 1993 Aug 15;151(4):2188-94.
5
Immunochemical properties of streptococcal M protein purified by isoelectric focusing.通过等电聚焦纯化的链球菌M蛋白的免疫化学特性
J Immunol. 1975 Oct;115(4):1002-6.
6
Streptococcal M6 protein expressed in Escherichia coli. Localization, purification, and comparison with streptococcal-derived M protein.在大肠杆菌中表达的链球菌M6蛋白。定位、纯化及与链球菌来源的M蛋白的比较。
J Exp Med. 1984 Apr 1;159(4):1083-95. doi: 10.1084/jem.159.4.1083.
7
[T-proteins of Streptococcus pyogenes. I. Communication: Preparation of a serological type specific T1-antigen by ion exchange chromatography and its characterization (author's transl)].[化脓性链球菌的T蛋白。I. 通讯:通过离子交换色谱法制备血清学类型特异性T1抗原及其特性鉴定(作者译)]
Zentralbl Bakteriol A. 1980;246(4):475-88.
8
Studies on group A streptococcal M-proteins: purification of type 5 M-protein and comparison of its amino terminal sequence with two immunologically unrelated M-protein molecules.A组链球菌M蛋白的研究:5型M蛋白的纯化及其氨基末端序列与两种免疫无关的M蛋白分子的比较。
J Immunol. 1980 Jan;124(1):261-7.
9
Primary structure of protective antigens of type 24 streptococcal M protein.24型链球菌M蛋白保护性抗原的一级结构
J Biol Chem. 1980 Jul 10;255(13):6284-9.
10
Purification and properties of M protein extracted from group A streptococci with pepsin: covalent structure of the amino terminal region of type 24 M antigen.用胃蛋白酶从A群链球菌中提取的M蛋白的纯化及性质:24型M抗原氨基末端区域的共价结构
J Exp Med. 1977 Jun 1;145(6):1469-83. doi: 10.1084/jem.145.6.1469.

引用本文的文献

1
Immunologically reactive proteins of Streptococcus equi.马链球菌的免疫反应性蛋白
Infect Immun. 1985 Apr;48(1):29-34. doi: 10.1128/iai.48.1.29-34.1985.