On the determination of the molecular weight of protein subunits on Sephadex G-200 in the presence of detergent. Glutamate dehydrogenase

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Abstract
A standard curve was prepared by plotting the logarithm of the molecular weight of proteins against their elution volume on Sephadex G-200 in the presence of sodium dodecyl sulfate and p-hydroxymercuribenzoate, from which a linear relationship was obtained. Glutamate dehydrogenase was completely dissociated into its monomer subunits by incubation at room temperature in the column eluent for 24 h, and the elution volume of the monomer was determined. From this data, the monomer molecular weight of the subunit was found to be 47 500 ± 2500.

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