Kinetic Studies of Na+/K+-ATPase in Tissue Aerobic Thyroid Patients

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Al Samurai et al.

Abstract

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 .                                                                                             

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Kinetic Studies of Na+/K+-ATPase in Tissue Aerobic Thyroid Patients. Baghdad Sci.J [Internet]. 2019 Sep. 22 [cited 2024 Mar. 29];16(3(Suppl.):0740. Available from: https://bsj.uobaghdad.edu.iq/index.php/BSJ/article/view/4132
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How to Cite

1.
Kinetic Studies of Na+/K+-ATPase in Tissue Aerobic Thyroid Patients. Baghdad Sci.J [Internet]. 2019 Sep. 22 [cited 2024 Mar. 29];16(3(Suppl.):0740. Available from: https://bsj.uobaghdad.edu.iq/index.php/BSJ/article/view/4132

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