ABSTRACT
An analytical method for simultaneous determination of five quinolones in spicy soup was developed. Spicy soup samples were firstly extracted by EDTA-Mcllvaine buffer at pH 4, then purified and concentrated by a novel Packed fiber solid phase extraction ( PFSPE ) coulumn. The extracted liquid supernatant was loaded onto the column, rinsed with water, and then eluted with 2% ammoniated methanol. The mobile phase was methanol-water-phosphoric acid (25:75:0. 1, V/V, adjusting the pH to 2. 8 with triethylamine) . These analytes were quantified by high performance liquid chromatography-fluorimetric detector( HPLC-FLD) at excitation and emission wavelength of 280 nm and 450 nm respectively. Recoveries of spiked quinolone antibiotics in spicy soup were from 72 . 1% to 110 . 3% with intraday relative standard deviation (RSD) between 1. 6% and 4. 3% and inter-day RSD from 2. 0% to 4. 3%. Limit of detection (LOD) and limit of quantitation(LOQ) were from 1. 2 to 5. 4 μg/L and from 3. 9 to 18 μg/L, respectively. The method could be applied to determine the quinolones in spicy soup.
ABSTRACT
<p><b>OBJECTIVE</b>To examine the expression of the tau protein and microtubule-associated proteins in the testis interstitium of aged and young rats.</p><p><b>METHODS</b>Sprague-Dawley male rats were divided into a young group(6 months, n = 10) and an aged group(28 months, n = 10). The two steps immunohistochemistry method with the antibody against tau protein and MAP alpha was performed on the testis tissues of the rats.</p><p><b>RESULTS</b>The results showed that the immunoreactive cells of tau protein of the testis interstilial of the aged rats obviously increased(P < 0.001) than those of the young, while the immunoreactive cells of the microtubule-associated proteins decreased(P < 0.01) in the aged.</p><p><b>CONCLUSION</b>The changes in the expression of the tau protein and microtubule-associated proteins may be related to the aging process of the testis.</p>
Subject(s)
Animals , Male , Rats , Aging , Metabolism , Immunohistochemistry , Microtubule-Associated Proteins , Rats, Sprague-Dawley , Testis , Chemistry , tau ProteinsABSTRACT
AIM To develope a reversed phase high performance liquid chromatography method to determine free concentrations of morphine (M) in the solution of human haemoglobin (Hb). To study the binding of M to haemoglobin, and evaluate the binding parameters of M to Hb. METHODS An ultrafiltration technique was used to recover morphine from the samples. Morphine was analyzed using a kromasil column (150 mm?4 6 mm) and a mobile phase of 0 1% tyiethylamine methanol (75∶25,v/v). The mobile phase pH was adjusted to 7 0 by phosphoric acid. The detection was set at 283 nm. RESULTS The ultrafiltration recovery of morphine was 98 5%. The Hb binding of M was concentration dependent of Hb and M. There were single typed binding sites for M to human Hb. The parameters determined were 4 1 for N and 340 mol?L -1 for K when the concentration of M and Hb were added from 8 50?10 -5 ～1 17?10 -2 mol?L -1 and 1 29?10 -4 ～8 57?10 -4 mol?L -1 respectively. CONCLUSION An ultrafiltration technique has proved to be simple and rapid for free drug determination. It is suitable for drug protein binding study.