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Acetyl phosphate(lithium potassium) Sale

(Synonyms: 乙酰磷酸锂钾盐) 目录号 : GC60555

Acetylphosphate(lithiumpotassium)是一种内源性代谢产物。

Acetyl phosphate(lithium potassium) Chemical Structure

Cas No.:94249-01-1

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10mM (in 1mL DMSO)
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Sample solution is provided at 25 µL, 10mM.

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产品描述

Acetyl phosphate(lithium potassium) is an endogenous metabolite.

Chemical Properties

Cas No. 94249-01-1 SDF
别名 乙酰磷酸锂钾盐
Canonical SMILES O=P([O-])([O-])OC(C)=O.[K+].[Li+]
分子式 C2H3KLiO5P 分子量 184.06
溶解度 Water: 50 mg/mL (271.65 mM) 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 5.433 mL 27.1651 mL 54.3301 mL
5 mM 1.0866 mL 5.433 mL 10.866 mL
10 mM 0.5433 mL 2.7165 mL 5.433 mL
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Research Update

Potassium fluxes in dialyzed squid axons

J Gen Physiol 1969 Jun;53(6):704-40.PMID:5795918DOI:10.1085/jgp.53.6.704.

Measurements have been made of K influx in squid giant axons under internal solute control by dialysis. With [ATP](i) = 1 microM, [Na](i) = 0, K influx was 6 +/- 0.6 pmole/cm(2) sec; an increase to [ATP](i) = 4 mM gave an influx of 8 +/- 0.5 pmole/cm(2) sec, while [ATP](i) 4, [Na](i) 80 gave a K influx of 19 +/- 0.7 pmole/cm(2) sec (all measurements at approximately 16 degrees C). Strophanthidin (10 microM) in seawater quantitatively abolished the ATP-dependent increase in K influx. The concentration dependence of ATP-dependent K influx on [ATP](i), [Na](i), and [K](o) was measured; an [ATP](i) of 30 microM gave a K influx about half that at physiological concentrations (2-3 mM). About 7 mM [Na](i) yielded half the K influx found at 80 mM [Na](i). The ATP-dependent K influx responded linearly to [K](o) from 1-20 mM and was independent of whether Na, Li, or choline was the principal cation of seawater. Substances tested as possible energy sources for the K pump were Acetyl phosphate, phosphoarginine, PEP, and d-ATP. None was effective except d-ATP and this substance gave 70% of the maximal flux only when phosphoarginine or PEP was also present.

Electrical potential accelerates the E1P(Na)----E2P conformational transition of (Na,K)-ATPase in reconstituted vesicles

J Biol Chem 1986 Sep 25;261(27):12437-40.PMID:3017974doi

We have used renal (Na,K)-ATPase, covalently labeled with fluorescein, and phospholipid vesicles reconstituted with labeled enzyme, to detect conformational transitions induced by Acetyl phosphate in the presence of Mg2+ and Na+ ions. Equilibrium fluorescence measurements show quenching of the fluorescein fluorescence, which is thought to reflect conversion of the initial E1 form to the phosphorylated E2P form. These fluorescence changes occur on inside-out-oriented pumps. The rates of acetyl phosphate-induced fluorescence changes have been measured using a stopped-flow fluorimeter. The rate of fluorescence quenching (1.5-3 s-1) is a measure of the rate of the E1P(Na)----E2P transition. The quenching is preceded by a fast fluorescence increase (12.3 +/- 4 s-1) associated with phosphorylation of E1 to E1P(Na), shown clearly in experiments with enzyme treated with oligomycin. Oligomycin greatly reduces the rate of the fluorescence quenching (0.044 +/- 0.01 s-1). Using potassium-loaded vesicles treated with valinomycin or lithium-loaded vesicles treated with Li+ ionophore N,N'-diheptyl-N,N'-didiethyl ether, 5,5-dimethyl-3,7-dioxanonanediamide in order to induce electrical diffusion potentials, negative inside, the rates of the fluorescence quenching are accelerated by up to 4-fold. The experiments demonstrate that the conformational transition E1P(Na)----E2P, associated with transport of 3 Na+ ions, is a voltage-sensitive reaction, carrying a net positive charge. This confirms a prediction based on transport experiments. In experiments with fluorescein-labeled (Na,K)-ATPase, the use of Acetyl phosphate rather than ATP, which does not bind, provides a valuable tool to detect fluorescence signals accompanying steps in the turnover cycle.