Magnesium chloride, active

Fig. 26. Activation of ATPase of actomyosin gel by magnesium chloride. Activation is expressed as percentage of the maximal, as obtained with 5 X 10 M CaCL. Curve, ATPase activity X superpreoipitation O solution of the gel (from Banga, 1942).

A mixture consisting of 0.69 g (10.5 mmoles) of zinc-copper couple, 12 ml of dry ether, and a small crystal of iodine, is stirred with a magnetic stirrer and 2.34 g (0.7 ml, 8.75 mmoles) of methylene iodide is added. The mixture is warmed with an infrared lamp to initiate the reaction which is allowed to proceed for 30 min in a water bath at 35°. A solution of 0.97 g (2.5 mmoles) of cholest-4-en-3/ -ol in 7 ml of dry ether is added over a period of 20 min, and the mixture is stirred for an additional hr at 40°. The reaction mixture is cooled with an ice bath and diluted with a saturated solution of magnesium chloride. The supernatant is decanted from the precipitate, and the precipitate is washed twice with ether. The combined ether extracts are washed with saturated sodium chloride solution and dried over anhydrous sodium sulfate. The solvent is removed under reduced pressure and the residue is chromatographed immediately on 50 g of alumina (activity III). Elution with benzene gives 0.62 g (62%) of crystalline 4/5,5/5-methylene-5 -cholestan-3/5-ol. Recrystallization from acetone gives material of mp 94-95° Hd -10°. 

Insertion of a longer spacer is compatible with antifungal activity. Reaction of epichlorohydrin with 4-chlorobenzyl-magnesium chloride leads to substituted phenylbutane Dis-... 

By melting the calculated amounts of magnesium and tin in an iron crucible under a mixture of potassium and magnesium chlorides, and cooling slowly, a mass of magnesium stannide was obtained from which individual crystals could be cleaved. The X-ray data were obtained from Laue and spectral photographs, treated as described by Dickinson.3 I wish to express my thanks to Dr. Roscoe G. Dickinson for his advice and active interest in this research. 

C. Active magnesium. A 200-ml., three-necked, round-bottomed flask is equipped with a Teflon-coated magnetic stirring bar, stopper, rubber septum, and condenser connected to an argon inlet (Note 6). The flask is charged with 1.5 g. (0.038 mole) of freshly cut potassium (Notes 7 and 8), 2.01 g. (0.0211 mole) of anhydrous magnesium chloride (Note 9), 3.55 g. (0.0214 mole) of anhydrous potassium iodide (Note 10), and 50 ml. of tetrahydrofu-ran (Note 11). The mixture is stirred vigorously (Note 12) and... 

The methylene group of anthrone 64 is acidic by virtue of doubly vinylic activation by the carbonyl group. Thus, treatment with methyl iodide and base leads to the 9,9-dimethyl derivative 65. Grignard reaction with 6-dimethylaminopropyl magnesium chloride... 

Characteristic properties of endopectate lyases are the high pH optimum, and a requirement for Ca2+ ions in order to maintain catalytic activity. The pH optimum of various endopectate lyases ranges from 8.0 to 9.5 (Refs. 4, 178, 234, 236, 243). Besides activation by Ca2+ ions, the optimal concentration of which is 1 mM,234,236,244 strontium salts were also considered in the case of Bacillus sp. lyase.234 The enzyme from Pseudomonas sp. was also partly activated by magnesium chloride,178 and for the lyase of Clostridium felsineum, salts of other bivalent cations had an activating effect as well.245 (Ethylenedinitrilo)tetraacetic acid completely inactivated all of the lyases mentioned. The activity of endopectate lyase from Pseudomonas was also lessened in the presence of sodium chloride, potassium chloride, and dipotassium hydrogen phosphate (K2HP04). 

The 1970s saw the introduction of higher activity catalysts based on magnesium chloride-supported titanium that improved the control of the physical properties of the polyethylene—molecular weights, stereospecificity, and the degree of copolymerization. 

Felsby S, Nielsen J, Arendtnielsen L, Jensen TS (1996) NMDA receptor blockade in chronic neuropathic pain a comparison of ketamine and magnesium chloride. Pain 64 283-291 Ferraguti F, Baldani-Guerra B, Corsi M, Nakanishi S, Corti C (1999) Activation of the extracellular signal-regulated kinase 2 by metabotropic glutamate receptors. Eur J Neurosci 11 2073-2082... 

Sample powders were dried in a vacuum oven at 60 C for 7 hours and cooled to minimize the hysteresis effect prior to storage in the dessicators of various water activities. In addition to Drierite, five saturated salt solutions were used in dessicators. These salt solutions were lithium chloride, magnesium chloride, potassium carbonate, sodium nitrite and potassium chloride. Their water activities were 0.110, 0.330, 0.440, 0.650 and 0.850, respectively, at 20 C. Each sample contained 1.2 to 1.5 g powder and four-week equilibration time was employed. The percentage of... 

Phosphate buffer (0.6 M) slightly inhibited lipolysis, but the same concentration of borate and barbiturate buffers was without effect. Zinc chloride, potassium cyanide, manganese sulfate, cysteine, and magnesium chloride retarded milk lapse activity to various degrees. All of these compounds were tested at pH 8.5 with tributyrin as substrate during a 30-min incubation period (Peterson et al 1948). 

The enzyme was purified from Candida utilis in 1965 by Rosen et al. (8Q). Dried yeast was allowed to autolyze in phosphate buffer at pH 7.5 for 48 hr, and the enzyme was isolated in crystalline form from these autolysates by a procedure which included heating to 55° at pH 5.0, fractionation with ammonium sulfate, and purification on phospho-cellulose columns from which the enzyme was specifically eluted with malonate buffer containing 2.0 mM FDP. Crystallization was carried out by addition of ammonium sulfate in the presence of mM magnesium chloride. The Candida enzyme was more active than the mammalian FDPases at room temperature and pH 9.5 the crystalline protein catalyzed the hydrolysis of 83 /nnoles of FDP per minute per milligram of protein. The enzyme was completely inactive with other phosphate esters, including sedoheptulose diphosphate, ribulose diphosphate, and fructose 1- or fructose 6-phosphates. Nor was the activity of the enzyme inhibited by any of these compounds. Optimum activity was observed at concentrations of FDP between 0.05 and 0.5 mM higher concentrations of FDP (5 mM) were inhibitory. 

The precipitation of protodolomite under 100°C. from solutions of calcium and magnesium chlorides has been reported, and it seems plausible to suggest that, given sufficient time, dolomite would result from recrystallization of protodolomite. Siegel (35) found that protodolomite was produced at 25 °C. when calcium and magnesium ions were entrapped in activated charcoal and could react with carbonate ion at a low rate he also found that sulfate ion was involved in dolomite formation. 

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