THE EFFECT OF AL(3+) AND HG(2+) ON GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM CAPOETA UMBLA KIDNEY
Date
2016Author
Kirici, M. and Demir, Y. and Beydemir, S. and Atamanalp, M.
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Glucose 6-phosphate dehydrogenase (EC 1.1.1.49; G6PD) is an important
enzyme found in all mammal tissues, and produces NADPH in the
metabolism. NADPH provides a reductive potential to maintain a balanced
redox state within the cell. The aim of this study was to purify G6PD
from Capoeta umbla kidney and determination of inhibition or activation
effects of aluminium and mercury on enzyme activity. In this purpose,
glucose 6-phosphate dehydrogenase was purified from Capoeta umbla kidney
by using preparation of homogenate, ammonium sulphate precipitation and
2',5'-ADP Sepharose 4B affinity chromatography. Molecular weight of the
enzyme was determined on sodium dodecyl sulphate-polyacrylamide gel
electrophoresis (SDS-PAGE) and the purified enzyme showed a single band
on the gel with a molecular weight of 75 kDa. Moreover, K-i constants of
Al3+ and Hg2+ were found as 0.98 +/- 0.084 and 0.57 +/- 0.019 mM,
respectively. In conclusion, affinity of the Hg2+ to the enzyme was
higher than Al3+
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