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对从肺炎克雷伯菌K43 - BTS1中分离出的一种与强直性脊柱炎HLA - B27阳性患者细胞发生交叉反应的因子的生化研究。

Biochemical studies on a factor isolated from Klebsiella K43-BTS1 that cross-reacts with cells from HLA-B27 positive patients with ankylosing spondylitis.

作者信息

Upfold L I, Sullivan J S, Geczy A F

出版信息

Hum Immunol. 1986 Nov;17(3):224-38. doi: 10.1016/0198-8859(86)90274-0.

Abstract

A component of the cell walls of certain enteric bacteria has been identified that cross-reacts with an HLA-B27-associated cell-surface structure on lymphocytes and other cell types from patients with ankylosing spondylitis. This component, or "modifying factor," from one particular organism, Klebsiella K43-BTS1, has been studied in detail. A purification scheme has been developed using preparative electrofocusing and gel-permeation high performance liquid chromatography techniques and the purified material used in various characterization studies. A previous study demonstrated that the modifying factor has an approximate molecular weight of 30,000 and an isoelectric point of 5.4-5.5. In this study two-dimensional gel electrophoresis experiments demonstrated that the modifying factor is associated with a single protein component of the cell wall of this organism. Pronase and papain destroyed the modifying factor activity whereas trypsin and alpha-chymotrypsin degraded the factor into smaller fragments without destroying its ability to modify B27+ AS- lymphocytes. Neuraminidase did not affect the modifying factor itself but did affect B27+ AS- lymphocytes such that they became unresponsive to modification. Sugar inhibition studies suggested that sugar groups are probably not involved in the function of the modifying factor. The availability of purified modifying factor should permit more detailed chemical analyses as well as functional studies to determine the significance of this molecule to the pathogenesis of ankylosing spondylitis.

摘要

已鉴定出某些肠道细菌细胞壁的一种成分,它能与强直性脊柱炎患者淋巴细胞和其他细胞类型上与HLA - B27相关的细胞表面结构发生交叉反应。来自一种特定生物体——肺炎克雷伯菌K43 - BTS1的这种成分或“修饰因子”已得到详细研究。已开发出一种纯化方案,使用制备性电聚焦和凝胶渗透高效液相色谱技术,并将纯化后的物质用于各种特性研究。先前的一项研究表明,该修饰因子的分子量约为30000,等电点为5.4 - 5.5。在本研究中,二维凝胶电泳实验表明,该修饰因子与该生物体细胞壁的单一蛋白质成分相关。链霉蛋白酶和木瓜蛋白酶会破坏修饰因子的活性,而胰蛋白酶和α - 胰凝乳蛋白酶会将该因子降解成较小的片段,但不会破坏其修饰B27 + AS - 淋巴细胞的能力。神经氨酸酶不会影响修饰因子本身,但会影响B27 + AS - 淋巴细胞,使其对修饰无反应。糖抑制研究表明,糖基团可能不参与修饰因子的功能。纯化修饰因子的可得性应能使人们进行更详细的化学分析以及功能研究,以确定该分子对强直性脊柱炎发病机制的意义。

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