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- W2014704416 abstract "Bovine liver glutamate dehydrogenase was covalently bound to porous succinamidopropyl-glass beads. Like native enzyme, the immobilized enzyme was subject to activation by ADP and inhibition by GTP, but such allosteric modulation was found to be fully reversible and not dependent on the association-dissociation proclivities of the “active monomeric” species." @default.
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- W2014704416 title "Reversible allosteric modulation of activity of immobilized hepatic glutamate dehydrogenase" @default.
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- W2014704416 doi "https://doi.org/10.1016/s0006-291x(74)80399-2" @default.
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