The ultrastructural effect and subcellular localization of mercuric chloride and methylmercuric chloride in insect cells (Aedes albopictusC6/36)

1999 ◽  
Vol 31 (2) ◽  
pp. 223-232 ◽  
Author(s):  
B.Braeckman, H. Raes
Keyword(s):  
Subcellular Localization ◽  
Mercuric Chloride ◽  
Insect Cells ◽  
Methylmercuric Chloride ◽  
Ultrastructural Effect

Differential effects of methylmercuric chloride and mercuric chloride on the L-glutamate and potassium evoked release of [3H]dopamine from mouse striatal slices

1986 ◽  
Vol 64 (5) ◽  
pp. 656-660 ◽  
Author(s):  
S. J. McKay ◽  
J. N. Reynolds ◽  
W. J. Racz
Keyword(s):  
Calcium Channel ◽  
Glutamate Receptor ◽  
Mercuric Chloride ◽  
Neurotransmitter Release ◽  
Mechanisms Of Action ◽  
Major Site ◽  
Striatal Slices ◽  
Differential Effects ◽  
Methylmercuric Chloride ◽  
Site Of Action

The effects of CH3HgCl and HgCl2 on the evoked release of 3H from mouse striatal slices prelabelled with [3H]dopamine have been examined. CH3HgCl (10 μM) was observed to increase the L-glutamate-evoked release of [3H]dopamine, while HgCl2 (10 μM) had no effect. In contrast, CH3HgCl at concentrations up to 100 μM had no effect on the 25 mM K+-stimulated release of [3H]dopamine, whereas HgCl2 (100 μM) significantly reduced the 25 mM K+-stimulated release of [3H]dopamine. Thus CH3HgCl and HgCl2 have differential effects on the L-glutamate- and K+-stimulated release of [3H]dopamine from mouse striatal slices, suggesting that these compounds may have different sites and (or) mechanisms of action in altering neurotransmitter release. It is suggested that CH3HgCl may act predominantly at intracellular sites or at the level of the L-glutamate receptor, whereas the major site of action of HgCl2 may be the voltage-operated calcium channel.

scholarly journals In vivo subcellular localization of Mal de Río Cuarto virus (MRCV) non-structural proteins in insect cells reveals their putative functions

Virology ◽  
2012 ◽  
Vol 430 (2) ◽  
pp. 81-89 ◽  
Author(s):  
Guillermo A. Maroniche ◽  
Vanesa C. Mongelli ◽  
Gabriela Llauger ◽  
Victoria Alfonso ◽  
Oscar Taboga ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Insect Cells ◽  
Structural Proteins

EFFECTS OF ACID, BASE, AND AMMONIUM SULFATE ON THE PROTEIN-BINDING PROPERTIES OF METHYLMERCURY IN CYTOPLASMIC PREPARATIONS FROM AVIAN LIVER AND KIDNEY

1973 ◽  
Vol 53 (4) ◽  
pp. 647-651
Author(s):  
R. S. BUSH ◽  
R. R. MARQUARDT
Keyword(s):  
Ammonium Sulfate ◽  
Perchloric Acid ◽  
Mercuric Chloride ◽  
Total Mercury ◽  
Acid Base ◽  
Binding Properties ◽  
Methylmercuric Chloride ◽  
Percent Protein ◽  
Liver And Kidney ◽  
Total Tissue

Commercial chick starter diets containing 4 ppm Hg added as mercuric chloride or 5 ppm Hg added as methylmercuric chloride were fed to chicks starting at 1 day of age and continuing for 4 wk. The intracellular and total mercury levels of liver and kidney from birds fed each diet and the effects of treatments with NaOH, with HCl, with perchloric acid, and with ammonium sulfate and of dialysis on protein-bound cytoplasmic methylmercury were determined. Livers and kidneys from chicks fed mercuric chloride contained three times more mercury than the control, whereas those from chicks fed methylmercuric chloride contained 15 times greater concentrations than controls. The microsomes and cytoplasm from chicks fed all diets contained approximately 5 and 55% of the total tissue mercury, respectively. Dialysis of kidney cytoplasm removed 50% of the total mercury. No appreciable dissociation of an ammonium sulfate-precipitated protein–mercury complex occurred when this was dissolved in water and treated with ammonium sulfate, perchloric acid, or NaOH, whereas HCl treatment dissociated 45% of the protein-bound mercury into the supernatant. When liver cytoplasm samples were made more alkaline, a greater proportion of the total mercury was found in the protein fraction. Acidification also increased the percent protein-bound mercury to a maximum at pH 1.5, followed by a linear decrease at pH levels below 1.5.

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