Abstract
A ribonucleotide reductase has been purified to homogeneity from Euglena gracilis. The enzyme will reduce the four common ribonucleoside triphosphates when a dithiol and 5′-deoxyadenosylcobalamin, required for activity, are added. Magnesium ions can stimulate the reaction. CTP reduction can be stimulated by dATP or ATP, and can be inhibited, as can ATP and GTP reduction, by dTTP. Reduction of UTP is unaffected by deoxyribonucleotides. The molecular weight of the enzyme from Euglena, as determined from gel filtration, is 440,000. Sodium dodecyl sulfate gels indicate subunits of approximately 100,000.
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