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- W1493768015 abstract "Abstract The effects of specific ligands on the intersubunit interactions in aspartate transcarbamylase of Escherichia coli were studied by treating the enzyme with low concentrations (up to 0.5 mm) of sodium dodecyl sulfate (SDS). The detergent was used to amplify the tendency of certain ligands to relax the oligomeric structure, by converting this relaxation to actual dissociation into subunits. The effect was measured by the increase in catalytic activity at subsaturating aspartate concentrations, known to accompany dissociation into subunits. The extent of dissociation was evaluated by column chromatography using Sephadex G-200. The following observations were made. (a) Ligands binding at the active sites such as orthophosphate, carbamyl phosphate, aspartate (in the presence of orthophosphate), and succinate (in the presence of carbamyl phosphate), in this order, enhanced the dissociating effect of the detergent. (b) A linear correlation was found between the extent of dissociation and the product of the net charge and molecular volume of these ligands. (c) All these ligands also protected the dissociated catalytic subunit against SDS inactivation. (d) The allosteric activator, ATP, and inhibitor, CTP, both stabilized the oligomeric structure, and prevented SDS-induced dissociation. (e) The allosteric effectors also protected the enzyme against heat-induced dissociation. These observations are shown to support the functional allosteric model recently proposed for this enzyme (Markus, G., McClintock, D. K., and Bussel, J. B. (1971) J. Biol. Chem. 246, 762)." @default.
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- W1493768015 date "1972-06-01" @default.
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- W1493768015 title "Conformational Changes in Aspartate Transcarbamylase" @default.
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- W1493768015 doi "https://doi.org/10.1016/s0021-9258(19)45109-0" @default.
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