This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bharier, M. Articles by Allis, D. Search for Related Content PubMed PubMed Citation Articles by Bharier, M. Articles by Allis, D.

Purification and Characterization of Axial Filaments from Treponema phagedenis Biotype reiterii (the Reiter Treponeme)

^a Department of Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267

ABSTRACT

Axial filaments have been purified from Treponema phagedenis biotype reiterii (the Reiter treponeme) and partially characterized chemically. The preparations consist largely of protein but also contain small amounts of hexose (3%). Filaments dissociate to subunits in acid, alkali, urea, guanidine, and various detergents. Amino acid analyses show an overall resemblance to other spirochetal axial filaments and to bacterial flagella. Dissociated filaments migrate as a single band upon acrylamide gel electrophoresis at pH 4.3 (in 4 M urea and 10 ³ M ethylenediaminetetraacetate) and at pH 12, but in sodium dodecyl sulfate gels, three bands are obtained under a wide variety of conditions. Two of these bands migrate very close together, with molecular weights of 33,000 ± 500. The other band has a molecular weight of 36,500 ± 500. Analysis of axial filaments by the dansyl chloride method yields both methionine and glutamic acid as amino terminal end groups. Sedimentation equilibrium measurements on dissociated axial filaments in 7 M guanidine hydrochloride yield plots of log C against ² which vary with the speed and initial protein concentration used. Molecular weight values calculated from these plots are consistent with a model in which axial filament subunits are heterogeneous with respect to molecular weight in the approximate range of 32,000 to 36,000.

¹ Present address: Department of Zoology, Indiana University, Bloomington, Ind. 47401.

This article has been cited by other articles:

• Downey, P. (2006). Profile of C. David Allis. Proc. Natl. Acad. Sci. USA 103: 6425-6427 [Full Text]