M Brunen

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The major outer membrane protein (Omp34) of Acidovorax delafieldii (formerly Pseudomonas delafieldii) was purified to homogeneity and was characterized biochemically and functionally. The polypeptide has an apparent molecular weight (Mr) of 34,000, and it forms stable oligomers at pH 9.0 in the presence of 10% octylpolyoxyethylene or 2% lithium dodecyl(More)
The functional properties of the major outer-membrane protein of Acidovorax delafieldii, the anion-selective porin Omp34, were investigated in artificial membranes. Detergent-solubilized porin incorporates into the membrane in a undirectional orientation solely determined by protein features. This enabled us to characterize the vectorial properties of the(More)
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