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. 1978 Dec;136(3):1127–1134. doi: 10.1128/jb.136.3.1127-1134.1978

Heat-modifiable outer membrane proteins of Neisseria meningitidis and their organization within the membrane.

C E Frasch, L F Mocca
PMCID: PMC218548  PMID: 102633

Abstract

Neisseria meningitidis group B serotype 2 strain M986 contains two predominant outer membrane proteins, with apparent molecular weights of 41,000 (protein b) and 28,000 (protein e). Heating of outer membrane vesicles at 56 degrees C for 20 min caused much of b** to disaggregate and denature into b (41,000 daltons). In contrast, protein e could be rapidly solubilized by SDS at room temperature into its monomeric state (e*), but it was not converted to its final higher apparent molecular weight of 28,000 (e) unless heated at 100 degrees C for 2 min. We propose that protein b exists in the membrane as trimers or tetramers in a transmembrane configuration and that protein e exists as subunits on the exterior surface of the outer membrane and has a highly ordered tertiary structure.

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These references are in PubMed. This may not be the complete list of references from this article.

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