Isolation of the aspartokinase domain of bifunctional aspartokinase I-homoserine dehydrogenase I from E.coli K12 |
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Authors: | M Veron Y Guillou G N Cohen |
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Affiliation: | Unité de Biochimie Cellulaire, Département de Biochimie et Génétique Moléculaire, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France |
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Abstract: | A proteolytic fragment (Mr approximately 25 000) carrying only the aspartokinase activity has been purified by chromatofocusing after limited proteolysis of aspartokinase I-homoserine dehydrogenase I from E.coli K12. The NH2-terminal sequence shows that it corresponds to the amino terminal peptide of the native enzyme. The results confirm a previous hypothesis about the organization of native aspartokinase I-homoserine dehydrogenase I. |
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