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1979 (1)
1Author    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