Isolation of the aspartokinase domain of bifunctional aspartokinase I‐homoserine dehydrogenase I from E.coli K12
- 25 February 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 181 (2), 381-384
- https://doi.org/10.1016/0014-5793(85)80297-0
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.Keywords
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