阴沟肠杆菌外膜中两种孔蛋白的纯化与特性分析
Purification and characterization of two kinds of porins from the Enterobacter cloacae outer membrane.
作者信息
Kaneko M, Yamaguchi A, Sawai T
出版信息
J Bacteriol. 1984 Jun;158(3):1179-81. doi: 10.1128/jb.158.3.1179-1181.1984.
Abstract
Two major outer membrane proteins of Enterobacter cloacae 206 were purified and identified as porins by using reconstituted vesicles. The 37-kilodalton porin forms a channel with a radius of 0.6 nm, which prefers positively charged substances to negatively charged ones, whereas the 39- to 40-kilodalton porin forms a larger channel with a radius of 0.8 nm, which has weaker selectivity for electric charges.
摘要
阴沟肠杆菌206的两种主要外膜蛋白被纯化，并通过重组囊泡鉴定为孔蛋白。37千道尔顿的孔蛋白形成一个半径为0.6纳米的通道，该通道更倾向于带正电荷的物质而非带负电荷的物质，而39至40千道尔顿的孔蛋白形成一个半径为0.8纳米的更大通道，其对电荷的选择性较弱。
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