IONIC SELECTIVITY OF PORES FORMED BY THE MATRIX PROTEIN (PORIN) OF ESCHERICHIA-COLI
IONIC SELECTIVITY OF PORES FORMED BY THE MATRIX PROTEIN (PORIN) OF ESCHERICHIA-COLI
复制标题
DOI:
10.1016/0005-2736(89)90002-3
复制
发表时间:
1979-01-01
期刊:
影响因子:
--
通讯作者:
LAUGER, P
中科院分区:
文献类型:
--
作者:
BENZ, R;JANKO, K;LAUGER, P
Incorporation of the matrix protein (porin) from the outer membrane of E. coli into black lipid films results in the formation of ion-permeable pores with a single-pore conductance of 2 nS (in 1 M KCl). Information on the structure of this pore was obtained by determining the selectivity of various ion species differing in charge and size. From the permeability of the pore for large organic ions (Tris+, glucosamine+, Hepes- [2-[-4-(2-hydroxyethyl)-1-piperra zinyl]-ethanesulfonic acid]) a minimum pore diameter of 0.8 nm is estimated. At neutral pH the pore is 2-4 times more permeable for alkali ions than for chloride. Based on the observed pH dependence of permeability, this cationic selectivity is explained by the assumption that the pore contains fixed negative charges.