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'Calcium Transport ATPase' in keywords
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1985 (1)
1982 (1)
1Author    P. Ankaj, M. Edda, W. Ilhelm, H. AsselbachRequires cookie*
 Title    Formation and Decay of the Vanadate Complex of the Sarcoplasmic Reticulum Calcium Transport Protein  
 Abstract    The calcium free sarcoplasmic reticulum calcium transport ATPase incorporates in the presence of magnesium ions approx. 8 nmol monovanadate per mg protein, indicating the formation of a complex containing one vanadate residue per enzyme molecule. On ligand-removal or dilution, the saturated enzyme complex displays biphasic decay kinetics, while the unsaturated complex slowly dissociates monophasically. — Ligand competition by raising the concentrations of un­ labeled vanadate results in a progressive decrease of the dissociation rate of the unsaturated enzyme. The complicated dissociation kinetics indicate a sequential mode of interaction between two ligand binding sites. The one to one stoichiometry of the complex suggests that the two sites are located at adjacent ATPase molecules. — It appears unlikely that the decay of the enzyme, vanadate complex is retarded by the formation of a stable quaternary complex between the enzyme, magnesium, mono-and polyvanadate. 
  Reference    Z. Naturforsch. 40c, 876 (1985); received August 23 1985 
  Published    1985 
  Keywords    Sarcoplasmic Reticulum, Calcium Transport ATPase, Vanadate 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0876.pdf 
 Identifier    ZNC-1985-40c-0876 
 Volume    40 
2Author    W. Ilhelm Hasselbach, Hans Liidi, Andrea MigalaRequires cookie*
 Title    Inactivation o f the Sarcoplasm ic Reticulum C alcium -Transport-A TPase by L asolocid in Com bination with Triton X-100  
 Abstract    The calcium-transport-ATPase of the sarcoplasmic reti­ culum membranes is irreversibly inactivated by the com­ bined action of Lasolocid and Triton X-100 at concentra­ tions which separately do not interfere with the enzyme's activity. In the presence of Lasolocid the enzyme is most susceptable to inactivation when the Triton X-100 concen­ tration just exceeds its critical micellar concentration, ~ 0.2 mg • ml-1. Lasolocid becomes effective at a concentra­ tion of 10 (jm and produces rapid inactivation at 100 |jm . The enzyme is more rapidly inactivated in the active than in the inactive state. 
  Reference    Z. Naturforsch. 37c, 1290—1292 (1982); received October 28 1982 
  Published    1982 
  Keywords    Calcium-Transport-ATPase, Sarcoplasmic Reticulum, Calcium-Ionophores, Triton X-100 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-1290_n.pdf 
 Identifier    ZNC-1982-37c-1290_n 
 Volume    37