Results 121 to 130 of about 2,495 (153)

ζ-Potential and surface charge of Thermoplasma acidophila

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1977
The surface charge density and the zeta-potential of Thermoplasma acidophila was estimated from microscopic electrophoresis experiments. The cells moved towards the positive electrode. The mobility remained constant from pH 2 to 5, and increased for pH values higher than 6.
J C, Hsung, A, Haug
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A new class of lipopolysaccharide from Thermoplasma acidophilum

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1974
Abstract A hot aqueous phenol extraction of lipid extracted whole cells of Thermoplasma acidophilum yielded a polymer that comprises 97% of the aqueous phase. The polymer is composed of 80% carbohydrate and 20% glycerol diether. Analysis of this polymer showed a ratio of 25:1:2 of carbohydrate: glycerol: alkane.
K J, Mayberry-Carson, T A, Langworthy, W R, MAyberry, P F, Smith   +3 more
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Primary Structure of the Thermosome fromThermoplasma acidophilum

Biological Chemistry Hoppe-Seyler, 1995
The thermosome, a chaperonin from the archaebacterium Thermoplasma acidophilum, consists of two subunits (M(r) 58,000 and 60,000) which assemble into a cylindrical complex of pseudo eight-fold rotational symmetry. The sequences of the two subunits are approximately 60% identical to each other and to TF55 from Sulfolobus shibatae, and are 30-40 ...
Waldmann, T., Lupas, A., Kellermann, J., Peters, J., Baumeister, W.   +4 more
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Biochemical properties of the proteasome from Thermoplasma acidophilum

European Journal of Biochemistry, 1992
We have purified proteasomes to apparent homogeneity from the archaebacterium Thermoplasma acidophilum. This proteinase has a molecular mass of about 650 kDa and an isoelectric point of 5.6. The proteasome hydrolyses peptide substrates containing an aromatic residue adjacent to the reporter group, as well as [14C]methylated casein optimally at pH 8.5 ...
Dahlmann, B., Kühn, L., Grziwa, A., Zwickl, P., Baumeister, W.   +4 more
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Superoxide dismutase from the archaebacterium Thermoplasma acidophilum

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1981
Thermoplasma acidophilum is a mycoplasma-like thermophilic organism that has been classified with the archaebacteria. It has a single superoxide dismutase (superoxide : superoxide oxidoreductase, EC 1.15.1.1) which is composed of four identically sized subunits.
K B, Searcy, D G, Searcy
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[A new species of Thermoplasma].

Wei sheng wu xue bao = Acta microbiologica Sinica, 1995
An extremely thermoacidophilic strain, ES-23, was isolated from a self-heating coal spoil pile, Sichuan, China. The new isolate grows between 50 and 75 degrees C with optimum 70 degrees C and pH 1.0-5.0 with optimum 2.0. Strain ES-23 is aerobic and facultative autotrophic depending both heterotrophically on organic compounds and autotrophically on ...
Y, Li, G, Liu, H, Zhong
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[52] Lipids of Thermoplasma

1982
Publisher Summary This chapter presents the procedures for the cultivation, isolation, and characterization of the diglyceryl tetraethers of Thermoplasma . Diglyceryl tetraethers are recovered from the nonsaponifiable fraction obtained by acid methanolysis of either whole cells, total lipids, or individual complex lipid species. Acid methanolysis is
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Thermoplasma acidophilum: Intracellular pH and potassium concentration

Biochimica et Biophysica Acta (BBA) - General Subjects, 1976
Thermoplasma acidophilum is a free-living thermophilic mycoplasma. Although the organism lacks a cell wall, it can grow in medium as dilute as 66 mosM. The intracellular K+ concentration can be as low as 17 mM, but varies according to the osmolality of the culture medium.
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Thermoplasma: a primordial cell from a refuse pile

Trends in Biochemical Sciences, 1982
Abstract A thermo-acidophilic archaebacterium is among the simplest of all known free-living microorganisms. Some of its features suggest that it might be related to the nucleus and cytoplasm of eukaryotic cells.
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Histone-like protein in the prokaryote Thermoplasma acidophilum

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1975
The DNA of the prokaryote Thermoplasma acidophilum is associated with a histone-like protein that has the following properties: it has a high content (23%) of basic amino acids, is positively charged at neutral pH, is soluble in acid, and can stabilize DNA against thermal denaturation.
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