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- W2124043504 abstract "The complex which is formed when excess regulatory subunits (r 2 ) of aspartate transcarbamoylase (EC 2.1.3.2) are added to a dilute solution of the catalytic subunit (c 3 ) has been studied by gel-filtration on Sephadex G-200. The elution volume indicates a Stokes' radius of between 5.42 and 5.92 nm, depending on the method of calculation. Using the sedimentation coefficient of 7.7 S previously determined, the molecular weight is estimated to be close to 200 000, in support of the c 3 r 6 structure proposed earlier for the complex. The calculated frictional coefficient indicates abnormal hydrodynamic properties which are probably due to unusual structure characteristics.The pattern of succinate inhibition of native aspartate transcarbamoylase has also been analyzed. At low concentrations, succinate activates the enzyme, presumably by converting it from the taut state to the relaxed (R) state. Further increase in the succinate concentration leads to competitive inhibition of the R state. Using a novel procedure for analysis of the data, the Michaelis constant for aspartate of the R state has been estimated to be about 7 mM. This value is close to the K m of c 3 r 6 for aspartate, measured under identical conditions. The result therefore provides further evidence suggesting that the c 3 r 6 complex resembles the R state of the native enzyme." @default.
- W2124043504 created "2016-06-24" @default.
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- W2124043504 date "1976-12-01" @default.
- W2124043504 modified "2023-09-26" @default.
- W2124043504 title "Further studies on aspartate transcarbamoylase: molecular weight of the c3r6 complex and analysis of succinate inhibition in the native enzyme" @default.
- W2124043504 doi "https://doi.org/10.1139/o76-155" @default.
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