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- W2003005087 abstract "Dehydroquinate synthase of Phaseolus mungo seedlings was purified 4400-fold from the (NH 4 ) 2 SO 4 fraction of a crude extract, the specific activity being 810 nkat per mg protein. When the purified enzyme was subjected to electrophoresis with or without sodium dodecyl sulfate, a single band was observed. The MW of the enzyme was estimated to be 67 000 by Sephadex G-100 gel chromatography and the minimum MW of the enzyme 43 000 by gel electrophoresis with sodium dodecyl sulfate. Atomic absorption analysis revealed that the purified enzyme contained small amounts of copper. Cobalt was not detected, although it has been implicated as a cofactor requirement." @default.
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- W2003005087 date "1980-01-01" @default.
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- W2003005087 title "Purification and metal requirements of 3-dehydroquinate synthase from Phaseolus mungo seedlings" @default.
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- W2003005087 doi "https://doi.org/10.1016/0031-9422(80)85109-0" @default.
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