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大鼠血清中具有补体抑制活性的α2-巨球蛋白的证据。

Evidence for an alpha 2-macroglobulin with complement-inhibiting activity in rat serum.

作者信息

Bellott R, Bon A, Lestage J, Giroud J P, Chateaureynaud P

机构信息

Département de Biologie du Développement, Université Bordeaux I, Paris, France.

出版信息

Int J Exp Pathol. 1991 Apr;72(2):151-61.

Abstract

alpha 2-Macroglobulin (alpha 2M) was purified both from the serum of male rats developing an acute turpentine-induced inflammatory reaction where its concentration is greatly increased (3-4 mg/ml) and from the serum of healthy males where it is present at low levels (15-30 micrograms/ml). A three-step purification procedure involving gel filtration, anion exchange chromatography on DEAE cellulose and negative immunoaffinity was used. A pure native alpha 2M, as assessed by biochemical and immunological tests, was obtained. This alpha 2M differed from other subforms in terms of its electric charge and its complement-inhibiting activity in a complement-dependent immune haemolysis test. Moreover, this inhibitory activity was not affected by complexing with trypsin or modification by interaction with methylamine showing that this newly described property is not linked to the well known antiproteinase function of alpha 2M.

摘要

α2-巨球蛋白(α2M)是从患急性松节油诱导炎症反应的雄性大鼠血清中纯化得到的,其浓度在该血清中大幅升高(3-4毫克/毫升),同时也从健康雄性大鼠血清中纯化得到,其在健康雄性大鼠血清中含量较低(15-30微克/毫升)。采用了三步纯化程序,包括凝胶过滤、DEAE纤维素阴离子交换色谱和阴性免疫亲和。通过生化和免疫测试评估,获得了纯的天然α2M。这种α2M在电荷及其在补体依赖性免疫溶血试验中的补体抑制活性方面与其他亚形式不同。此外,这种抑制活性不受与胰蛋白酶复合或与甲胺相互作用修饰的影响,表明这种新描述的特性与α2M众所周知的抗蛋白酶功能无关。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1882/2002297/35a46591317c/ijexpath00026-0052-a.jpg

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