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肠杆菌科两个不同属的菌毛抗原的纯化及理化分析:肠炎沙门氏菌和小肠结肠炎耶尔森氏菌(作者译)

[Purification and physico-chemical analysis of the fimbrial antigen in two different genera of Enterobacteriacea: Salmonella enteritidis and Yersinia enterocolitica (author's transl)].

作者信息

Aleksić S, Aleksić V

出版信息

Zentralbl Bakteriol Orig A. 1979 Apr;243(2-3):177-96.

PMID:377854
Abstract

Chemical, physical and immunological properties of the fimbrial antigen of two different genera of Enterobacteriaceae, namely Salmonella (S. enteritidis) and Yersinia (Y. enterocolitica) were analysed. Only a few strains of these two bacterial genera possess a fimbrial antigen which proved to be identical in all tests. Purified fimbriae are unstable in buffer solutions. They tend to form aggregates, patterns of which are between 240000 and 270000. Submitted to solubility testing by various methods these aggregates easily dissociate into particles of different molecular size. Treatment with 1% sodium dodecyl sulphate (SDS) in 1% mercaptoaethanol at 37 degrees C for 60 minutes gave constant reproducible results. The fimbrial protein prepared by this method proved to be an antigenically active unit with a molecular weight of 23450 for S. enteritidis and 23350 for Y. enterocolitica. The electron microscope revealed that purified fimbriae of these two genera consist of extremely thin filaments (1.5 to 2.7 nm), covering the bacterial cell as an envelope. They are supposed to be composed of no more than 2 to 3 peptid chains. The presence of the amino acids tyrosine, phenylalanine and tryptophane may be responsible of the particular behaviour of the fimbriae which according to different external conditions react with different states of dissociation. Probably the filaments are not stable in a solution as single filaments but tend to form oligomer, secondary and tertiary structures. Experiments of isoelectric focusing revealed that both antigens consist of a pure protein component (composed of 17 amino acids) which appears at pH 3.9.

摘要

对肠杆菌科两个不同属,即沙门氏菌(肠炎沙门氏菌)和耶尔森氏菌(小肠结肠炎耶尔森氏菌)的菌毛抗原的化学、物理和免疫学特性进行了分析。这两个细菌属中只有少数菌株拥有菌毛抗原,且在所有测试中都证明是相同的。纯化的菌毛在缓冲溶液中不稳定。它们倾向于形成聚集体,其模式在240000至270000之间。通过各种方法进行溶解度测试时,这些聚集体很容易解离成不同分子大小的颗粒。在37℃下用1%十二烷基硫酸钠(SDS)和1%巯基乙醇处理60分钟可得到恒定且可重复的结果。用这种方法制备的菌毛蛋白被证明是一种抗原活性单位,肠炎沙门氏菌的分子量为23450,小肠结肠炎耶尔森氏菌的分子量为23350。电子显微镜显示,这两个属的纯化菌毛由极细的细丝(1.5至2.7纳米)组成,像包膜一样覆盖着细菌细胞。它们应该由不超过2至3条肽链组成。氨基酸酪氨酸、苯丙氨酸和色氨酸的存在可能是菌毛特殊行为的原因,根据不同的外部条件,菌毛会以不同的解离状态发生反应。可能这些细丝在溶液中作为单丝时不稳定,而是倾向于形成寡聚体、二级和三级结构。等电聚焦实验表明,两种抗原都由一种纯蛋白质成分(由17种氨基酸组成)组成,该成分出现在pH 3.9处。

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