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Abstract
Purified glutamate synthase from Escherichia coli has been disaggregated with sodium dodecylsulfate and resolved into two non-identical subunits (molecular weights 135 000 and 53 000) using agarose gel filtration in the presence of sodium dodecylsulfate. The ratio between the content of the two subunits in the native enzyme is in agreement with the ratio between subunit molecular weights suggesting that the subunits occur in equal numbers in the native enzyme. Amino acid analysis and N-terminal analysis of the separate subunits confirm their nonidentity.
Published Version
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