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Open Access. Powered by Scholars. Published by Universities.®

2004

Turkish Journal of Medical Sciences

Erythrocytes

Articles 1 - 2 of 2

Full-Text Articles in Medicine and Health Sciences

The Effects Of Melatonin On 6-Phosphogluconate Dehydrogenase: An In Vitro And In Vivo Study, İlhami̇ Gülçi̇n, Şükrü Beydemi̇r Jan 2004

The Effects Of Melatonin On 6-Phosphogluconate Dehydrogenase: An In Vitro And In Vivo Study, İlhami̇ Gülçi̇n, Şükrü Beydemi̇r

Turkish Journal of Medical Sciences

Melatonin is known to influence a variety of biological processes including circadian rhythms, neuroendocrine, and cardiovascular and immune functions as well as thermoregulation. Melatonin is the chief secretory product of the pineal gland, although it is also produced in other organs. In this study, in vitro effects of melatonin on 6-phosphogluconate dehydrogenase from human erythrocytes and in vivo effects of melatonin on 6-phosphogluconate dehydrogenase from rat (Sprague-Dawley) erythrocytes were studied. Human erythrocyte 6-phosphogluconate dehydrogenase was purified in 3 steps, namely haemolysate preparation, ammonium sulphate fractionation (35-65%) and 2´,5´-ADP Sepharose-4B affinity gel chromatography. 6-Phosphogluconate dehydrogenase was purified with a recovery rate …


Recovery Of 1-Chloro-2,4-Dinitrobenzene Detoxification By N-Acetyl- L-Cysteine In Glutathione Predepleted Human Erythrocytes, Deni̇z Yildiz, C.Işil Kuran Jan 2004

Recovery Of 1-Chloro-2,4-Dinitrobenzene Detoxification By N-Acetyl- L-Cysteine In Glutathione Predepleted Human Erythrocytes, Deni̇z Yildiz, C.Işil Kuran

Turkish Journal of Medical Sciences

Glutathione is an important thiol-containing compound involved in the detoxification process in erythrocytes. Its thiol group reacts with a variety of xenobiotics in a glutathione S-transferase catalyzed reaction to form conjugates that are effluxed from the erythrocytes by an ATP dependent transport mechanism. A well studied experimental system is the transport of the conjugate of glutathione and 1-chloro-2,4-dinitrobenzene. We investigated whether N-acetyl-L-cysteine protects the free-SH content and restores 1-chloro-2,4-dinitrobenzene detoxification in erythrocytes or replaces glutathione in detoxification process in glutathione predepleted erythrocytes. Our results indicate that N-acetyl-L-cysteine restores the intracellular free-SH content following depletion by 1-chloro-2,4-dinitrobenzene and N-ethylmaleimide. N-acetyl-L-cysteine (10 …