Demonstration of (Ca2+-Mg2+-ATPase activity of the neural cell adhesion molecule
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چکیده
منابع مشابه
comparison of catalytic activity of heteropoly compounds in the synthesis of bis(indolyl)alkanes.
heteropoly acids (hpa) and their salts have advantages as catalysts which make them both economically and environmentally attractive, strong br?nsted acidity, exhibiting fast reversible multi-electron redox transformations under rather mild conditions, very high solubility in polar solvents, fairly high thermal stability in the solid states, and efficient oxidizing ability, so that they are imp...
15 صفحه اولRole of Mg2+ in the Ca2+-Ca2+ exchange mediated by the membrane-bound (Ca2+, Mg2+)-ATPase of sarcoplasmic reticulum vesicles.
Sarcoplasmic reticulum vesicles were preloaded with either 45Ca2+ or unlabeled Ca2+. The unidirectional Ca2+ efflux and influx, together with Ca2+-dependent ATP hydrolysis and phosphorylation of the membrane-bound (Ca2+, Mg2+)-ATPase, were determined in the presence of ATP and ADP. The Ca2+ efflux depended on ATP (or ADP or both). It also required the external Ca2+. The Ca2+ concentration depen...
متن کاملMorphometrical Study of Polysialylated Neural Cell Adhesion Molecule Positive Cells in Rat Pups Hippocampus Following Induction of Seizure during Pregnancy
Background:The polysialylated neural cell adhesion molecule (PSA-NCAM) is expressed in developing brain. Fetal brain damage is caused by different conditions such as seizure and hypoxia. The present study was designed to investigate the effect of maternal seizures on the number of PSA-NCAM positive cells in pup's hippocampus. Methods: Female Wistar rats were divided into four groups: (a) kindle...
متن کاملEffects of Mg2+, anions and cations on the Ca2+ + Mg2+-activated ATPase of sarcoplasmic reticulum.
In a previous paper [Gould, East, Froud, McWhirter, Stefanova & Lee (1986) Biochem. J. 237, 217-227] we presented a kinetic model for the activity of the Ca2+ + Mg2+-activated ATPase of sarcoplasmic reticulum. Here we extend the model to account for the effects on ATPase activity of Mg2+, cations and anions. We find that Mg2+ concentrations in the millimolar range inhibit ATPase activity, which...
متن کاملAllosteric modification by K+ of the (Ca2+ + Mg2+)-dependent ATPase of sarcoplasmic reticulum. Interaction with Mg2+.
The K’ activation profile of the (Cap+ + My’+)-dependent ATPase of sarcoplasmic reticulum vesicles is markedly changed by the free magnesium concentration. At 0.2 mM Mg’+, a complex dependence on the K+ concentration is observed which changes to a simple hyperbolic dependence when Mg’+ is raised to 3 mM. The degree of activation by K+ is always higher at 0.2 rnH than at 3 mM MgY+. At 0.2 mM Mg”...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1993
ISSN: 0014-5793
DOI: 10.1016/0014-5793(93)80820-k