Quinone Profiles of Thermoplasma acidophilum HO-62
نویسندگان
چکیده
منابع مشابه
Effects of pH and temperature on the composition of polar lipids in Thermoplasma acidophilum HO-62.
Thermoplasma acidophilum HO-62 was grown at different pHs and temperatures, and its polar lipid compositions were determined. Although the number of cyclopentane rings in the caldarchaeol moiety increased when T. acidophilum was cultured at high temperature, the number decreased at low pHs. Glycolipids, phosphoglycolipids, and phospholipids were analyzed by high-performance liquid chromatograph...
متن کاملComplete polar lipid composition of Thermoplasma acidophilum HO-62 determined by high-performance liquid chromatography with evaporative light-scattering detection.
Polar ether lipids of Thermoplasma acidophilum HO-62 were purified by high-performance liquid chromatography with an evaporative light-scattering detector. Structures of purified lipids were investigated by capillary gas chromatography, mass spectrometry, and nuclear magnetic resonance. Three types of ether lipids were found: phospholipids, glycolipids, and phosphoglycolipids. The two phospholi...
متن کاملScanning electron microscopy of Thermoplasma acidophilum.
The scanning electron microscope was utilized to observe the morphology of the thermophilic, acidophilic mycoplasma, Thermoplasma acidophilum. Upon examination of the surface morphology, the size and shape of this unusual mycoplasma revealed its similarity to the other mycoplasmas that have been investigated.
متن کاملUltrastructure of lipopolysaccharide isolated from Thermoplasma acidophilum.
The fine structure of lipopolysaccharide isolated from Thermoplasma acidophilum was examined by electron microscopy. Negative staining of the lipopolysaccharide revealed long, ribbon-like structures with some branching. The average width of the lipopolysaccharide ribbons was 5 nm. Treatment of the lipopolysaccharide with 0.5% sodium dodecyl sulfate resulted in the dissociation of the ribbon-lik...
متن کاملComplexes of the proteolytic machinery from Thermoplasma acidophilum
The tricorn protease has been described as the core of protein degradation in the archaeon Thermoplasma acidophilum, since it is processing products of the proteasome, which breaks down protein substrates in many organisms. Three tricorn interacting factors have the capacity to cleave the generated small oligopeptides with relatively broad specificity into free amino acids that are recycled in ...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2001
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.183.4.1462-1465.2001