Ethacrynic acid high-sensitive Mg-ATPase activity in brain microsomes

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Solubilization and separation of ethacrynic acid (EA) highly sensitive and EA less sensitive Mg2+-ATPases in the rat brain.

Rat brain microsomal Mg2+-ATPases with two distinct activities: ethacrynic acid (EA) highly sensitive and EA less sensitive Mg2+-ATPase activities were solubilized by the combined treatment with 10 mM 3-(3-chlolamidopropyl)-dimethylammonio-1-propane-sulfate (CHAPS) and 30 mM octyl-beta-D-glucoside. The solubilized enzymes had properties similar to those of the membrane-bound enzyme in microsome...

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High Affinity Ca 2 + - stimulated Mg 2 + - dependent ATPase in Rat Brain

High affinity Ca2+-stimulated Mga+-dependent ATPase activity of nerve ending particles (!vnaphmm) from rat brain tissue appears to be associated primarily with isolated synaptic plasma membranes. The synaptic membrane (Ca2+ + Mga+)-ATPase activity was found to exhibit strict dependence on Mg+ for the presence of the activity, a high affinity for Ca2+ (&.a = 0.23 NM), and relatively high affini...

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Effect of salts on the activity and inhibition of E. coli membrane ATPase by ethacrynic acid and inhibitors.

The [Mg, Ca] -ATPase activity of E. coli depends on the anion present and follows the chao­ tropic sequence: Acetate” > H C03~ > Cl> I ” > N 03~ > SCN”. There are only small differences between the different alkali chlorides. The [Mg, Ca]-ATPase was inhibited by all these salts when the ratio of Mg or Ca to ATP was 1: 5 at pH 9.1. At pH 9.1 or 7.5 and a Mg to ATP ratio of 1 some salts activate ...

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Sensitivity of the brain synaptosomal membrane Mg(2+)-ATPase activity to arachidonic acid is under control of the Na+,K(+)-ATPase state.

Evidence is presented for the sensitivity of the synaptosomal plasma membrane Mg(2+)-ATPase activity to arachidonic acid being dependent on the functional state of Na+,K(+)-ATPase. An "Inversion effect" was observed at arachidonic acid concentrations exceeding 80 mumol/l when the Mg(2+)-ATPase activity (after ouabain addition) is higher than the total ATPase activity (without ouabain). The "Inv...

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ژورنال

عنوان ژورنال: Japanese Journal of Pharmacology

سال: 1982

ISSN: 0021-5198

DOI: 10.1016/s0021-5198(19)54104-x