Abstract
The complex protein carrying the two threonine sensitive activities aspartokinase I and homoserine dehydrogenase I is composed of six subunits of a molecular weight 60,000. Furthermore, quantitative determination of the N‐terminal amino acids indicates the presence of six methionine residues per mole of native enzyme (mol. wt. 360,000).Equilibrium sedimentation studies of N‐ethylmaleimide treated protein shows that its six disulfide bridges, revealed by chemical analysis, are intra‐chain.Fingerprints of tryptic digests of the protein fail to reveal any difference between the subunits.
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