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. 1981 Jun;146(3):1083–1090. doi: 10.1128/jb.146.3.1083-1090.1981

Cell wall proteins of Aquaspirillum serpens.

S F Koval, R G Murray
PMCID: PMC216964  PMID: 6787011

Abstract

The Triton X-100-insoluble wall fraction of Aquaspirillum serpens VHA contained three major proteins: the regularly structured (RS) superficial protein (molecular weight 140,000) and two peptidoglycan-associated proteins (molecular weights, 32,000 and 33,000). The molecular arrangement and interactions of the outer membrane and RS proteins were examined with the use of bifunctional cross-linking reagents. The peptidoglycan-associated and RS proteins were not readily cross-linked in either homo- or heteropolymers. This suggests that the free amino groups are not suitably disposed for cross-linking. Some high-molecular-weight multimers of the RS protein were produced, but the subunit structure of the RS array was not stabilized by cross-linking. The peptidoglycan-associated proteins were cross-linked to high-molecular-weight multimers, but no dimers or trimers were produced. This result suggests that these proteins exist in the outer membrane as multimers larger than trimers.

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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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