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'Rhodospirillum rubrum' in keywords
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1998 (1)
1979 (2)
1Author    HansWerner Miiller, Margareta BaltscheffskyRequires cookie*
 Title    On the Oligomycin-Sensitivity and Subunit Composition of the ATPase Complex from Rhodospirillum rubrum  
 Abstract    Two alternative procedures for isolation of the oligomycin-sensitive ATPase complex (E. C. from R. rubrum chromatophores are compared with respect to ease, rapidity, and yield. The inhibitory effect of oligomycin on the membrane-bound Ca2+ -ATPase activity is increased during storage of the chromatophores, whereas the effect of oligomycin on the membrane-bound Mg2+ -ATPase activity does not change within a week. Oligomycin-sensitivity of the solubilized ATPase complex depends on the isolation procedure. The enzyme complex consists of at least nine different polypeptides with the apparent molec­ ular weights of (. The polypeptides 2 — 4, 7, and 8 represent subunits of coupling factor 1. 
  Reference    Z. Naturforsch. 34c, 229 (1979); received January 4 1979 
  Published    1979 
  Keywords    Rhodospirillum rubrum, ATPase, Subunits, Oligomycin 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0229.pdf 
 Identifier    ZNC-1979-34c-0229 
 Volume    34 
2Author    HansW. Erner Müller, Udo Schwuléra, Manfred Salzer, Klaus DoseRequires cookie*
 Title    Purification, Subunit Structure, and Kinetics of the Chloroform-Released FjATPase Complex from Rhodospirillum rubrum and Its Comparison with FjATPase Forms Isolated by Other Methods  
 Abstract    A stable and homogeneous adenosine-5'-triphosphatase (ATPase, EC has been solubilized from R hodospirillum rubrum (R . rubrum) chromatophores by chloroform extraction. Purification of the Ca2+-dependent ATPase activity was 200-fold. Ca2+ can be replaced by M g2+, Cd2+, and M n2+ .The K m for Ca-ATP (0.17 m M) is increased about 5-fold during solubilization of the enzyme, whereas the K m values for Mg-ATP (0.029 m M) and Cd-ATP (0.014 m M) are not affected. The chloroform-released A TPase has a molecular weight of 400,000 + 30,000 and consists of the following subunits (m olecular weights in parenthesis): a (58,000), ß (53,500), y (39,000), 6(18,500), and £(14,000). The amino acid composition and the fluorescence spectra are presented. Besides the chloroform-released A TPase complex three other Ca2+-dependent A T Pase forms have been isolated from R. rubrum chromatophores by other methods for comparison. Ultrasonica-tion of the m em branes leads to the release of an ATPase complex which is m ainly composed of a, ß , and 7 -subunits. From an acetone powder extract an A TPase complex could be purified by affinity chromatography which is composed of four kinds of subunits (a, ß , y, 6). The same acetone powder yields an A TPase consisting of only three different types of subunits (a, ß, y) if the final purification step is preparative disc electrophoresis on 6% polyacrylam ide gels instead of affinity chromatography. 
  Reference    Z. Naturforsch. 34c, 38 (1979); received November 10 1978 
  Published    1979 
  Keywords    Rhodospirillum rubrum, F xA TPase Complexes, Subunit Structure, Kinetics 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0038.pdf 
 Identifier    ZNC-1979-34c-0038 
 Volume    34 
3Author    Z. NaturforschRequires cookie*
 Title    The Rieske Protein from Purple Sulfur Bacteria Is an Extrinsic Protein  
 Abstract    The mode of membrane attachment of the Rieske iron-sulfur protein from cytochrome be, complex of Rhodospirillum rubrum has been studied using biochemical approaches. In contrast to cytochrome c, the bacterial Rieske protein was extracted from chromato-phores using chaotropic agents (NaSCN, urea, guanidine), an alkaline pH and relatively low concentration of Triton X-100. The results presented here lead to the conclusion, that the Rieske protein from chromato-phores is extrinsic and that their association with the rest of the complex involves hydropho­ bic interactions. In tro d u ctio n 
  Reference    Z. Naturforsch. 53c, 15—20 (1998); received September 30/0ctober 16 1997 
  Published    1998 
  Keywords    Chrom atophor, Cytochrome be, Complex, Rieske Protein, Rhodospirillum rubrum 
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 TEI-XML for    default:Reihe_C/53/ZNC-1998-53c-0015.pdf 
 Identifier    ZNC-1998-53c-0015 
 Volume    53