Na+/K+-ATPase is a prevalent enzyme that maintains the Na+ and K+ gradients across the cell membrane by transporting three Na+ out and two K+ into the cell, the aim of this study is to provide detailed mechanistic insights, potentially with important effects on physiological regulation of active Na and K transport in tissues of Aerobic Thyroid Patient. Thyroid tissues were obtained from a 35 year old patients, the operation was carried out at the Al-Hadi Specialist Hospital in Samarra city, the sample was stored at -20ºC until used. The purification protocol included Salt Precipitation, Ion Exchange Chromatography, Gel Filtration and Electrophoresis, a spectrophotometric method was used to determine the enzyme activity. kinetic parameters was also obtained for the enzyme. Partial purification of Na+/K+-ATPase revealed two isoenzymes (I ,II). The purity of separated isoenzymes were proved by SDS-PAGE electrophoresis. The kinetic characteristics of Na+/K+-ATPase showed that optimum substrate concentration about 1.5mM, Km 1.052mM, and Vmax 6.062, optimum temperature was 37 ºC, optimum pH 7.4 and optimum time in 25 min. Na+/K+-ATPase purified from Thyroid tissue has distinct kinetic characteristic that reflects the importance of intracellular regulation of specific Na+/K+-ATPase pump which gives cells the ability to precisely coordinate to their physiological requirements .
In this article four samples of HgBa2Ca2Cu2.4Ag0.6O8+δ were prepared and irradiated with different doses of gamma radiation 6, 8 and 10 Mrad. The effects of gamma irradiation on structure of HgBa2Ca2Cu2.4Ag0.6O8+δ samples were characterized using X-ray diffraction. It was concluded that there effect on structure by gamma irradiation. Scherrer, crystallization, and Williamson equations were applied based on the X-ray diffraction diagram and for all gamma doses, to calculate crystal size, strain, and degree of crystallinity. I
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