Halobacterium halobium

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J.p. Bhatt - One of the best experts on this subject based on the ideXlab platform.

Ignat Ignatov - One of the best experts on this subject based on the ideXlab platform.

  • improved method for isolation of photochrome transmembrane protein bacteriorhodopsin from purple membranes of Halobacterium Halobacterium halobium
    Journal of Medicine Physiology and Biophysics, 2015
    Co-Authors: Oleg Mosin, Ignat Ignatov
    Abstract:

    This paper presents improved method for isolation of photochrome transmembraine protein bacteriorhodopsin (output 5 mg from 100 g of wet biomass) capable to transform light energy to electrochemical energy of generated protons H + and ??P. The protein was isolated from purple membranes of photo-organotrophic Halobacterium Halobacterium halobium by cellular autolysis by distilled water, processing of bacterial biomass by ultrasound at 22 KHz, alcohol extraction of low and high-weight molecular impurities, cellular RNA, carotenoids and lipids, solubilization with 0.5% (w/v) SDS-Na, fractionation by MeOH and column g el permeation chromatography (GPC) of the final protein on Sephadex G-200 with 0.1% (w/v) SDS-Na and 2.5 mM ETDA. The homogeneity of the isolated BR was proved by combination of preparative and analytical methods including elecrtophoresis in 12.5% (w/v) PAAG with 0.1% (w/v) SDS-Na and regeneration of apomembranes with 13- trans -retinal. Keywords: Halobacterium halobium , purple membranes, bacteriorhodopsin, biosynthesis, biomolecular electronics

  • The Natural Phototransforming Photochrome Membrane Protein Bacteriorhodopsin From Purple Membranes of Halobacterium Halobacterium halobium
    Nanotechnology Research and Practice, 2014
    Co-Authors: Oleg Mosin, Ignat Ignatov
    Abstract:

    The article presents the technology of microbiological synthesis of natural phototransforming photochrome transmembraine protein bacteriorhodopsin (output 8-10 mg) from purple membranes of photo-organotrophic Halobacterium Halobacterium halobium, which is capable to transform light energy to electrochemical energy of generated protons H + and adenosine-5 ' -triphosphate (АТP). These data are important for nanoindustry of new modern domestic phototransforming nanomaterials on the base of bacteriorhodopsin and molecular bioelectronics.

  • photochrome transmembrane protein bacteriorhodopsin from purple membranes of Halobacterium halobium in nano and biotechnologies
    Journal of Medicine Physiology and Biophysics, 2014
    Co-Authors: Oleg Mosin, Ignat Ignatov
    Abstract:

    This paper presents improved method for isolation of photochrome transmembraine protein bacteriorhodopsin (output 5 mg from 100 g of wet biomass) capable to transform light energy to electrochemical energy of generated protons H + and ??P. The protein was isolated from purple membranes of photo-organotrophic Halobacterium Halobacterium halobium by cellular autolysis by distilled water, processing of bacterial biomass by ultrasound at 22 KHz, alcohol extraction of low and high-weight molecular impurities, cellular RNA, carotenoids and lipids, solubilization with 0.5% (w/v) SDS-Na, fractionation by MeOH and column g el permeation chromatography (GPC) of the final protein on Sephadex G-200 with 0.1% (w/v) SDS-Na and 2.5 mM ETDA. The homogeneity of the isolated BR was proved by combination of preparative and analytical methods including elecrtophoresis in 12.5% (w/v) PAAG with 0.1% (w/v) SDS-Na and regeneration of apomembranes with 13- trans -retinal. Keywords: Halobacterium halobium , purple membranes, bacteriorhodopsin, biosynthesis, biomolecular electronics

  • isolation of photochrome transmembrane protein bacteriorhodopsin from purple membranes of Halobacterium Halobacterium halobium new method for isolation
    Journal of Health Medicine and Nursing, 2014
    Co-Authors: Oleg Mosin, Ignat Ignatov
    Abstract:

    This paper presents improved method for isolation of photochrome transmembraine protein bacteriorhodopsin (output 5 mg from 100 g of wet biomass) capable to transform light energy to electrochemical energy of generated protons H + and ??P. The protein was isolated from purple membranes of photo-organotrophic Halobacterium Halobacterium halobium by cellular autolysis by distilled water, processing of bacterial biomass by ultrasound at 22 KHz, alcohol extraction of low and high-weight molecular impurities, cellular RNA, carotenoids and lipids, solubilization with 0.5% (w/v) SDS-Na, fractionation by MeOH and column g el permeation chromatography (GPC) of the final protein on Sephadex G-200 with 0.1% (w/v) SDS-Na and 2.5 mM ETDA. The homogeneity of the isolated BR was proved by combination of preparative and analytical methods including elecrtophoresis in 12.5% (w/v) PAAG with 0.1% (w/v) SDS-Na and regeneration of apomembranes with 13- trans -retinal. Keywords: Halobacterium halobium , purple membranes, bacteriorhodopsin, biosynthesis, biomolecular electronics

  • Halobacterium Halobacterium halobium. Biosynthesis of Deuterium-labeled Transmembrane Protein bacteriorhodopsin from Halobacterium halobium
    Journal of Health Medicine and Nursing, 2014
    Co-Authors: Oleg Mosin, Ignat Ignatov
    Abstract:

    The semi-preparative biosynthesis of photochrome transmembrane protein bacteriorhodopsin (output 8 - 10 mg) , labeled with deuterium on functionally important amino acid residues - [2,3,4,5,6- 2 H 5 ]phenylalanine, [3,5- 2 H 2 ]tyrosine, and [2,4,5,6,7- 2 H 5 ]tryptophan was carried out with using a photo-organotrophic Halobacterium Halobacterium halobium . The protein was isolated from purple membranes by cellular autolysis by distilled water, processing of bacterial biomass by ultrasound at 22 KHz, alcohol extraction of low and high-weight molecular impurities, cellular RNA, carotenoids and lipids, with the subsequent s olubilization of final product with 0.5% (w/v) SDS-Na and fractionation by methanol. T he homogeneity of the synthesized product, and the selectivity of deuterium incorporation into the molecule was proved by combination of preparative and analytical protein methods including elecrtophoresis in 12.5% (w/v) PAAG with 0.1% (w/v) SDS-Na, gel filtration chromatography on Sephadex G-200, and electron impact mass-spectrometry of methyl esters of N-Dns-[ 2 H ]derivatives of amino acids after their separation by reverse-phase HPLC. Keywords : Halobacterium halobium, b acteriorhodopsin, [2,3,4,5,6- 2 H 5 ]Phe, [3,5- 2 H 2 ]Tyr, [2,4,5,6,7- 2 H 5 ]Trp, biosynthesis, EI mass-spectrometry, RP-HPLC.

M L Salin - One of the best experts on this subject based on the ideXlab platform.

  • Elevation of superoxide dismutase in Halobacterium halobium by heat shock.
    Journal of bacteriology, 1991
    Co-Authors: G B Begonia, M L Salin
    Abstract:

    Abstract Exposure of Halobacterium halobium to 50 degrees C for 2.5 h in an aerobic environment resulted in a greater than twofold increase in the activity of the manganese-containing superoxide dismutase. Nondenaturing polyacrylamide gels stained for enzymatic activity did not reveal any additional isozymes of superoxide dismutase induced by the heat shock. The maximal effect was observed at 50 degrees C, and the elevated levels of activity remained constant during 5 h of recovery at 40 degrees C. The induction of enzymatic activity was sensitive to protein synthesis inhibitors. The results are discussed relative to heat shock and stress-related proteins as well as alterations in metabolism brought about by elevated temperatures.

Janos K Lanyi - One of the best experts on this subject based on the ideXlab platform.

Oleg Mosin - One of the best experts on this subject based on the ideXlab platform.

  • improved method for isolation of photochrome transmembrane protein bacteriorhodopsin from purple membranes of Halobacterium Halobacterium halobium
    Journal of Medicine Physiology and Biophysics, 2015
    Co-Authors: Oleg Mosin, Ignat Ignatov
    Abstract:

    This paper presents improved method for isolation of photochrome transmembraine protein bacteriorhodopsin (output 5 mg from 100 g of wet biomass) capable to transform light energy to electrochemical energy of generated protons H + and ??P. The protein was isolated from purple membranes of photo-organotrophic Halobacterium Halobacterium halobium by cellular autolysis by distilled water, processing of bacterial biomass by ultrasound at 22 KHz, alcohol extraction of low and high-weight molecular impurities, cellular RNA, carotenoids and lipids, solubilization with 0.5% (w/v) SDS-Na, fractionation by MeOH and column g el permeation chromatography (GPC) of the final protein on Sephadex G-200 with 0.1% (w/v) SDS-Na and 2.5 mM ETDA. The homogeneity of the isolated BR was proved by combination of preparative and analytical methods including elecrtophoresis in 12.5% (w/v) PAAG with 0.1% (w/v) SDS-Na and regeneration of apomembranes with 13- trans -retinal. Keywords: Halobacterium halobium , purple membranes, bacteriorhodopsin, biosynthesis, biomolecular electronics

  • The Natural Phototransforming Photochrome Membrane Protein Bacteriorhodopsin From Purple Membranes of Halobacterium Halobacterium halobium
    Nanotechnology Research and Practice, 2014
    Co-Authors: Oleg Mosin, Ignat Ignatov
    Abstract:

    The article presents the technology of microbiological synthesis of natural phototransforming photochrome transmembraine protein bacteriorhodopsin (output 8-10 mg) from purple membranes of photo-organotrophic Halobacterium Halobacterium halobium, which is capable to transform light energy to electrochemical energy of generated protons H + and adenosine-5 ' -triphosphate (АТP). These data are important for nanoindustry of new modern domestic phototransforming nanomaterials on the base of bacteriorhodopsin and molecular bioelectronics.

  • photochrome transmembrane protein bacteriorhodopsin from purple membranes of Halobacterium halobium in nano and biotechnologies
    Journal of Medicine Physiology and Biophysics, 2014
    Co-Authors: Oleg Mosin, Ignat Ignatov
    Abstract:

    This paper presents improved method for isolation of photochrome transmembraine protein bacteriorhodopsin (output 5 mg from 100 g of wet biomass) capable to transform light energy to electrochemical energy of generated protons H + and ??P. The protein was isolated from purple membranes of photo-organotrophic Halobacterium Halobacterium halobium by cellular autolysis by distilled water, processing of bacterial biomass by ultrasound at 22 KHz, alcohol extraction of low and high-weight molecular impurities, cellular RNA, carotenoids and lipids, solubilization with 0.5% (w/v) SDS-Na, fractionation by MeOH and column g el permeation chromatography (GPC) of the final protein on Sephadex G-200 with 0.1% (w/v) SDS-Na and 2.5 mM ETDA. The homogeneity of the isolated BR was proved by combination of preparative and analytical methods including elecrtophoresis in 12.5% (w/v) PAAG with 0.1% (w/v) SDS-Na and regeneration of apomembranes with 13- trans -retinal. Keywords: Halobacterium halobium , purple membranes, bacteriorhodopsin, biosynthesis, biomolecular electronics

  • isolation of photochrome transmembrane protein bacteriorhodopsin from purple membranes of Halobacterium Halobacterium halobium new method for isolation
    Journal of Health Medicine and Nursing, 2014
    Co-Authors: Oleg Mosin, Ignat Ignatov
    Abstract:

    This paper presents improved method for isolation of photochrome transmembraine protein bacteriorhodopsin (output 5 mg from 100 g of wet biomass) capable to transform light energy to electrochemical energy of generated protons H + and ??P. The protein was isolated from purple membranes of photo-organotrophic Halobacterium Halobacterium halobium by cellular autolysis by distilled water, processing of bacterial biomass by ultrasound at 22 KHz, alcohol extraction of low and high-weight molecular impurities, cellular RNA, carotenoids and lipids, solubilization with 0.5% (w/v) SDS-Na, fractionation by MeOH and column g el permeation chromatography (GPC) of the final protein on Sephadex G-200 with 0.1% (w/v) SDS-Na and 2.5 mM ETDA. The homogeneity of the isolated BR was proved by combination of preparative and analytical methods including elecrtophoresis in 12.5% (w/v) PAAG with 0.1% (w/v) SDS-Na and regeneration of apomembranes with 13- trans -retinal. Keywords: Halobacterium halobium , purple membranes, bacteriorhodopsin, biosynthesis, biomolecular electronics

  • Halobacterium Halobacterium halobium. Biosynthesis of Deuterium-labeled Transmembrane Protein bacteriorhodopsin from Halobacterium halobium
    Journal of Health Medicine and Nursing, 2014
    Co-Authors: Oleg Mosin, Ignat Ignatov
    Abstract:

    The semi-preparative biosynthesis of photochrome transmembrane protein bacteriorhodopsin (output 8 - 10 mg) , labeled with deuterium on functionally important amino acid residues - [2,3,4,5,6- 2 H 5 ]phenylalanine, [3,5- 2 H 2 ]tyrosine, and [2,4,5,6,7- 2 H 5 ]tryptophan was carried out with using a photo-organotrophic Halobacterium Halobacterium halobium . The protein was isolated from purple membranes by cellular autolysis by distilled water, processing of bacterial biomass by ultrasound at 22 KHz, alcohol extraction of low and high-weight molecular impurities, cellular RNA, carotenoids and lipids, with the subsequent s olubilization of final product with 0.5% (w/v) SDS-Na and fractionation by methanol. T he homogeneity of the synthesized product, and the selectivity of deuterium incorporation into the molecule was proved by combination of preparative and analytical protein methods including elecrtophoresis in 12.5% (w/v) PAAG with 0.1% (w/v) SDS-Na, gel filtration chromatography on Sephadex G-200, and electron impact mass-spectrometry of methyl esters of N-Dns-[ 2 H ]derivatives of amino acids after their separation by reverse-phase HPLC. Keywords : Halobacterium halobium, b acteriorhodopsin, [2,3,4,5,6- 2 H 5 ]Phe, [3,5- 2 H 2 ]Tyr, [2,4,5,6,7- 2 H 5 ]Trp, biosynthesis, EI mass-spectrometry, RP-HPLC.