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来自齿垢密螺旋体外膜的主要53千道尔顿表面抗原的成孔特性。

Pore-forming properties of the major 53-kilodalton surface antigen from the outer sheath of Treponema denticola.

作者信息

Egli C, Leung W K, Müller K H, Hancock R E, McBride B C

机构信息

Department of Microbiology, University of British Columbia, Vancouver, Canada.

出版信息

Infect Immun. 1993 May;61(5):1694-9. doi: 10.1128/iai.61.5.1694-1699.1993.

DOI:10.1128/iai.61.5.1694-1699.1993
PMID:7682993
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC280753/
Abstract

A 53-kDa protein from the outer sheath of the oral spirochete Treponema denticola was purified to homogeneity and shown to reconstitute channels in black lipid bilayer model membranes. The channel had a single-channel conductance of 1.8 nS in 0.1 M KCl, making this the largest porin channel observed to date (estimated diameter, 3.4 nm). Electron micrographs of 53-kDa-protein-containing outer sheaths of T. denticola showed a regular hexagonal array of darker staining pits.

摘要

从口腔螺旋体齿垢密螺旋体的外鞘中纯化出一种53 kDa的蛋白质,使其达到同质状态,并证明它能在黑色脂质双层模型膜中重建通道。该通道在0.1 M KCl中的单通道电导为1.8 nS,这使其成为迄今为止观察到的最大的孔蛋白通道(估计直径为3.4 nm)。含有53 kDa蛋白质的齿垢密螺旋体外鞘的电子显微镜照片显示出规则的六边形排列的深色染色小孔。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/30e7/280753/9badd63bf23d/iai00017-0113-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/30e7/280753/f1ecc63db517/iai00017-0111-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/30e7/280753/9c9e6ec76c38/iai00017-0112-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/30e7/280753/9badd63bf23d/iai00017-0113-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/30e7/280753/f1ecc63db517/iai00017-0111-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/30e7/280753/9c9e6ec76c38/iai00017-0112-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/30e7/280753/9badd63bf23d/iai00017-0113-a.jpg

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