| Literature DB >> 9726928 |
Abstract
The open channel characteristics of the bacterial porin Omp32 from Comamonas acidovorans were investigated by means of conductance measurements in planar lipid bilayers of the Montal-Mueller type. Particularly at low salt conditions (< or = 30 mM KCl) Omp32 exhibited some unusual asymmetric and nonlinear functional properties. Current-voltage relationship measurements showed that conductance depends on the orientation of porin molecules and is a nonlinear function of the applied membrane potential. Conductance also depends on the salt concentration in a manner not common to porins and the salt concentration modulates the nonlinearity of conductance-voltage relationships. Omp32 is strongly anion-selective. The nonlinear and asymmetric conductance of the open channel is a new observation in porins.Entities:
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Year: 1998 PMID: 9726928 PMCID: PMC1299801 DOI: 10.1016/S0006-3495(98)74045-7
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033