Glutamate potassium

SYNS l-GLCTAMIC ACID, MONOPOTASSIUM SALT xMONOPOTASSIUM 1-GLUTAMATE (FCC) MPG POTASSIUM GLUTAMATE POTASSIUM GLUT-AMINATE... 

In their natural environment, bacterial cells need to adapt to a wide range of osmotic conditions. Escherichia coli cells exposed to hypo-osmotic shock respond by a rapid release of cellular osmolytes such as proline, potassium glutamate, trehalose, and ATP. This ability prevents the cells from lysis by decreasing the turgor pressure on the challenge of a sudden shift in osmolarity. Bacterial MS channels, MscL and MscS (Fig. la and b), are major components of adaptation mechanisms to hypo-osmotic shock. Being located in the cytoplasmic membrane, MscL and MscS are activated by an increase of membrane tension... 

Another important issue concerns the intracellular buffers used. We have obtained good results with a potassium glutamate/HEPES buffer (see below). Whenever it might be important, the concentrations of free calcium ions have to be carefully controlled by the use of chelators. As the active concentration of free calcium for exocytosis in insulin-secreting cells ranges from 0.1 (xM (basal) to 10 xM (maximal stimulatory levels) with an EC50 at 2 xM, EGTA is a suitable chelator (Vallar ef ai, 1987). 

Fig. 2. Acidification of small synaptic vesicles by glutamate and chloride in synap-tosomes. The acidification assay was performed as described in section 3.2 of this chapter. Two representative experiments with intact (upper trace) or SLO-permeabilized (lower trace) synaptosomes are shown. The ordinate gives the changes of absorbance obtained (A 492-530). Final concentrations of potassium glutamate (Glut), KCl, and ammonium sulfate (NH/) were 10 mM, 45 mM and 30 mM, respectively. The uptake of glutamate and chloride result in an acidification of the lumen of small synaptic vesicles, which increases the vesicular uptake of acridine orange, resulting in a decrease in the amount of extravesicular dye. This acidification can be only observed when the plasma membrane is permeabilized...

Potassium glutamate (622) L-Monopotassium L-glutamate Flavor enhancer salt substitute ADI not specified ... 

Saponin solution (140 mM potassium glutamate-HCl, pH 6.8, with 1 mg/mL ATP and 0.1 mg/mL saponin) for the intact cell-binding assay. 

In the contrast to the S. shibatae enzyme, the P. furiosus DNA topoisomerase VI needs the presence of a protein stabilizer in the reaction medium. In the absence of 0.5 M potassium glutamate, no activity was detectable. This strong stabilization effect of potassium glutamate has already been observed for other extreme... 

Fig. 6. Effect of ZnCl2 and potassium glutamate (KGIu) on double-stranded DNA thermodegradation (neutral gel). To test the effect of ZnCl2, plasmid pTZlS was incubated for 30 min at 95° in 50 mM Tris buffer, pH 7.5 (room temperature). To lest the effect of KGIu, plasmid pTZI8 was incubated for 1 hr at 95° in 25 mM Tris buffer, pH 7.5 (room temperature), c. Control without incubation at high temperature DFII, dimer of form II.

L-Glutamic acid, monopotassium salt. See Potassium glutamate... 

Monopotassium glutamate Monopotassium L-glutamate. See Potassium glutamate Monopotassium 2-hydroxypropanoate acid. 

P-Anisic acid Guazatine Nonanoyl 4-hydroxy-3-methoxybenzylamide replenisher Potassium glutamate reprographic paper... 

C5H8KNO4 H2O (monohydrate) Potassium glutamate C5H8NNa04 H2O (monohydrate)... 

Cold denaturation is an interesting phenomenon that results from hydration of polar and nonpolar proteins and weakening of hydrophobic forces, all of which have a significant effect on protein folding and stability. Intracellular enzymes from psychrophiles are protected from cold denaturation by compatible solutes, such as potassium glutamate and trehalose (67). Psychrophiles also have intracellular cold shock proteins that act as chaperones, cryoprotectors, and antifreeze molecules. There is no explanation yet for protection from cold denaturation for extracellular psychrophilic enzymes, but exopolymeric substances may be involved (67). 

Dynamin GTPase activity was measured essentially by the method of Barylko (2001). GTPase assay was performed in cytosolic buffer (25 mM Hepes-KOH, pH 7.2, 25 mM KCl, 2.5 mM magnesium acetate, 100 mM potassium glutamate) in 2.0 ml microcentrifuge tubes. One hundred /ul of reaction mixture contained protein and lipid at the following concentrations. 

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