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在吐温20或脱氧胆酸钠存在的情况下,对莱氏无胆甾原体纯化膜蛋白进行交叉免疫电泳。

Crossed immunoelectrophoresis, in the presence of tween 20 or sodium deoxycholate, of purified membrane proteins from Acholeplasma laidlawii.

作者信息

Johansson K E, Wróblewski H

出版信息

J Bacteriol. 1978 Oct;136(1):324-30. doi: 10.1128/jb.136.1.324-330.1978.

Abstract

Five membrane proteins from Acholeplasma laidlawii have been previously purified on a large scale. These proteins have been used to establish the relationship between the precipitation lines obtained by crossed immunoelectrophoresis of solubilized cell membrane proteins from A. laidlawii in the presence of the neutral detergent Tween 20 or those obtained in the presence of the anionic detergent sodium deoxycholate. This relationship, which was unambiguously established for four of the five proteins, was determined by tandem or "parallel" crossed immunoelectrophoresis of the sodium deoxycholate-solubilized membrane together with the purified proteins. Membranes from strain A of A. laidlawii were composed of proteins, which were immunologically related to and probably identical to membrane proteins from strain B of this organism.

摘要

此前已大规模纯化了来自莱氏无胆甾原体的五种膜蛋白。这些蛋白已被用于确定在中性去污剂吐温20存在下,莱氏无胆甾原体溶解细胞膜蛋白经交叉免疫电泳得到的沉淀线与在阴离子去污剂脱氧胆酸钠存在下得到的沉淀线之间的关系。这五种蛋白中的四种蛋白的这种关系已明确确立,它是通过脱氧胆酸钠溶解的膜与纯化蛋白的串联或“平行”交叉免疫电泳来确定的。莱氏无胆甾原体A菌株的膜由蛋白质组成,这些蛋白质与该生物体B菌株的膜蛋白在免疫上相关且可能相同。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f42c/218664/3d2d325f703d/jbacter00287-0334-a.jpg

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