PubMed · 8713886
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A M Griffin, H G Griffin. 1996. A rapid plasmid purification method for dideoxy sequencing.. https://doi.org/10.1385/0-89603-402-x%3A367
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The effect of piroxicam in three different formulations was tested on rabbits for 28 days in an alkali burn model. The ulceration healing process was determined by evaluating the severity of the burn (scored from 0 to 5), and the re-epithelization healing process was measured by the area of the defects. The results indicated that the piroxicam positively charged submicron emulsion was the most effective formulation in lowering the ulcerative cornea score while the piroxicam positively charged emulsion and the blank emulsion were more effective in promoting the re-epithelization healing process. The piroxicam solution elicited the slowest healing re-epithelization rate after 28 days and was unable to complete the entire healing process. The new positively charged submicron emulsion formulation of piroxicam had a pronounced effect on both the ulceration rate and epithelial defects in the management of corneal alkali-burning.
The role of external HCO3- in pHi regulation in rat mast cells was studied with BCECF. In a HCO3--free medium cells undergo an alkalinization after the addition of 40 mM HCO3Na. This alkalinization is unaffected by pH. In a Na+-free medium, the addition of 20 mM HCO3Na induced a higher alkalinization than 20 mM HCO3K. Amiloride (1 mM), a Na+/H+ exchanger inhibitor, inhibited by 45% the alkalinization induced by HCO3Na, but it did not change that induced by HCO3K. The anion exchanger inhibitor DIDS reduced 20% the alkalinization induced by both salts. An alkalinization of 0.085 units is observed after the addition of 20 mM HCO3K, even when these exchangers are inhibited (in the absence of Na+ and presence of DIDS). We conclude that the Na+/H+ exchanger and the Cl-/HCO3- exchangers are alkalinizing mechanisms that regulate pHi in these cells. Also, there is some HCO3--dependent, Na+-independent mechanism responsible for the intracellular alkalinization.
Although a seemingly simple concept, sample volume and the reaction vessel size are important considerations when undertaking an alkaline hydrolysis of a phosphoprotein, particularly if the phosphoamino acid of interest is either phosphohistidine or phosphotyrosine. It should be noted that the experiments conducted in this article used large concentrations of both phosphotyrosine and the most stable form of phosphohistidine (8), which highlights the problems that may be faced during phosphoamino acid analysis of a protein sample that contains only small amounts of either phosphoamino acid. Although not tested, it is likely that similar hydrolysis effects may occur for phospholysine. If the reaction volume is to be kept to a minimum and the alkaline digestion is from either a membrane blot or in solution, then the use of a mineral oil overlay should be considered to prevent concentration of the alkali and hydrolysis of the phosphate moiety.