ZfN: Search Results

1	Author	P. Ankaj, M. Edda, W. Ilhelm, H. Asselbach	Requires 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

2	Author	W. Ilhelm Hasselbach, Hans Liidi, Andrea Migala	Requires 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