Purification and some catalytic properties of phosphoglucomutase from maize leaves

Abstract

Phosphoglucomutase (EC 2.7.5.1, PGM) was purified to homogeneity from maize (Zea mays L.) leaves. The enzyme had specific activity 11. 7 U/mg protein and molecular mass (determined by gel-chromatography) of 133 +/- 4 kD. The molecular mass of PGM subunits determined by SDS-electrophoresis was 66 +/- 3 kD. The enzyme had Km for glucose-1-phosphate and… (More)

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@article{Popova1998PurificationAS, title={Purification and some catalytic properties of phosphoglucomutase from maize leaves }, author={Popova and Matasova and Lapot'ko}, journal={Biochemistry. Biokhimiia}, year={1998}, volume={63 6}, pages={697-701} }