Outer membrane porin protein of Haemophilus influenzae type b: pore size and subunit structure.

Abstract:

:The 40-kDa porin protein of Haemophilus influenzae type b was reconstituted into proteoliposomes. The relative rates of diffusion of small uncharged sugars across the channels formed by this protein were determined by measuring the rates of osmotic swelling of the liposomes. From these rates, a pore diameter of 1.8 nm was estimated using the Renkin equation. A chemical cross-linking technique was used to investigate the oligomeric structure of the 40-kDa porin. Sodium dodecyl sulfate - polyacrylamide gel electrophoresis revealed the presence of porin dimers and trimers after reaction of the protein with dithio-bis-(succinimidyl propionate). These results confirmed that the porin of H. influenzae forms large water-filled channels and indicated that it probably exists as trimers in the outer membrane.

journal_name

Can J Microbiol

authors

Vachon V,Kristjanson DN,Coulton JW

doi

10.1139/m88-027

subject

Has Abstract

pub_date

1988-02-01 00:00:00

pages

134-40

issue

2

eissn

0008-4166

issn

1480-3275

journal_volume

34

pub_type

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