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On the activity of glucose-6-phosphate phosphohydrolase in the red blood cells

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Summary

Glucose-6-phosphatase activity is demonstrated in the human, rat and rabbit red blood cells. This activity was about 50% higher in the reticulocytes than in the red blood cells. The optimal pH for this activity was of about 6.5 and optimal temperature 37.5°C. Glucose-6-phosphatase activity was inhibited by amytal and p-chlor-mercury-benzoate (PCMB), showing the possible presence in the structure of essential-SH and flavin groups. After inhibition with PCMB, partial reactivation is obtained with glutathione and cysteine. Enzymatic activity appears to play an important role in the resynthesis of glucose and regulation of glycolysis by hydrolysis of glucose-6-phosphate, a specific inhibitor ofhexokinase.

Zusammenfassung

Die Glucose-6-Phosphatase-Aktivität wird an den Erythrozyten des Menschen, der Ratte und dem Kaninchen gezeigt. Diese Aktivität war bei den Retikulozyten um 50% höher als bei den Erythrozyten. Das pH-Optimum dieser Aktivität betrug ca. 6,5 und die optimale Temperatur 37,5°C. Die Glucose-6-Phosphatase-Aktivität wurde mit Amytal und PCMB inhibiert, um in der Struktur die eventuell vorhandenen essentiellen SH- und Flavingruppen zu zeigen. Nach der Inhibition mit PCMB wird eine Teilreaktivierung mit GSH und Cystein erhalten. Die Enzym-Aktivität scheint eine wichtige Rolle bei der Resynth ese der Glucose und der Regulation der Glykolyse durch Hydrolyse des Glykose-6-Phosphats, einem spezifischen Inhibitor der Hexokinase, zu spielen.

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Ababei, L., Moisiu, M. On the activity of glucose-6-phosphate phosphohydrolase in the red blood cells. Blut 20, 363–369 (1970). https://doi.org/10.1007/BF01634046

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