作者: L S Thomashow , S C Rittenberg
DOI: 10.1128/JB.163.3.1047-1054.1985
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摘要: Abstract A procedure was developed for the purification of sheathed flagella from Bdellovibrio bacteriovorus 109J. Preparations isolated appeared as filaments 28 nm in diameter, did not vary sheath content by more than 10% mean, and contained 50% protein, 38% phospholipid, 12% lipopolysaccharide (LPS) weight. The readily solubilized Triton X-100, whether or EDTA present, all LPS phospholipid 30 to 40% protein intact flagella; sedimentable core filament polypeptides accounted remainder. Flagellar significantly enriched nonadecenoic acid (19:1) depleted beta-hydroxymyristic relative outer membrane intraperiplasmically grown bdellovibrios. These observations suggest that is a stable domain distinct bulk membrane. also substantially (57%) less (26%) heterogeneous composition previously described membranes. This unusual balance constituents predicted result fluid compatible with model generation motility rotation within highly flexible sheath.