| Literature DB >> 3512520 |
T E Fehniger, J D Radolf, M A Lovett.
Abstract
Ultrastructural and biochemical studies of a recombinant Treponema pallidum surface antigen designated 4D have been conducted due to its likely biological significance. Electron microscopy demonstrated that the 190-kilodalton (kDa) 4D molecule is an ordered ring structure of 10-nm diameter. The 90-kDa proteinase K-treated 4D is an ordered ring structure of 6-nm diameter. Evidence is presented that the 190-kDa ordered ring is maintained by noncovalent bonds; 19-kDa monomers can reassociate in vitro to reform a 190-kDa molecule. Amino acid composition analysis of 190-kDa 4D showed that the molecule is composed of 45% hydrophobic residues. Evidence relating the structure of the 4D ordered ring to its potential role in the pathogenesis of syphilis is discussed.Entities:
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Year: 1986 PMID: 3512520 PMCID: PMC214490 DOI: 10.1128/jb.165.3.732-739.1986
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490