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Isolelectric focusing of human red blood cell glutathione reductase saturated and unsaturated with flavin-adenin-dinucleotid

Isoelektrische Fokussierung von Glutathionreductase menschlicher Erythrocyten bei unterschiedlicher Bindung des Co-Fakters Flavin Adenin Dinucleotid

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Summary

Human glutathione reductase (E.C.1.6.4.2.) was purified from red blood cells and flavin-adenine-dinucleotide (FAD) was stripped off partially by acid treatment. Isoelectric focusing studies of the untreated enzyme revealed three zones with enzymatic activity at pH 6.75, 7.1 and 7.45 whereas the acid treated preparations showed an additional peak at pH 8.0 whose enzymatic activity was increased about twofold by FAD. We conclude that this fraction represents an enzyme unsaturated with FAD.

Zusammenfassung

Glutathionreductase (E.C.1.6.4.2.) wurde von menschlichen Erythrocyten angereichert und FAD durch Säurebehandlung abgespalten. Die Auftrennung des nativen Enzyms durch isoelektrisches Focussieren ergab 3 Zonen mit enzymatischer Aktivität bei pH 6.75, 7.1 und 7.45. Die säurebehandelte Präparation zeigte einen zusätzlichen Gipfel bei pH 8.0, dessen enzymatische Aktivität durch FAD auf das doppelte stimuliert werden konnte. Wir schließen daraus, daß die pH 8-Fraktion einem Enzym entspricht, das statt 2 FAD Moleküle nur 1 FAD gebunden enthält.

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References

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Authors and Affiliations

  1. I. Medizinische Klinik der Universität Hamburg, Germany

    H. W. Rüdiger

  2. Medizinische Klinik der Universität Freiburg, Germany

    K. G. Blume, H. Arnold & G. W. Löhr

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  1. H. W. Rüdiger
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  2. K. G. Blume
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  3. H. Arnold
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  4. G. W. Löhr
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This work was supported by a grant from the Deutsche Forschungsgemeinschaft.

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Rüdiger, H.W., Blume, K.G., Arnold, H. et al. Isolelectric focusing of human red blood cell glutathione reductase saturated and unsaturated with flavin-adenin-dinucleotid. Klin Wochenschr 52, 896–897 (1974). https://doi.org/10.1007/BF01468617

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  • DOI: https://doi.org/10.1007/BF01468617

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