Proteolysis of the bifunctional methionine-repressible aspartokinase II-homoserine dehydrogenase II of Escherichia coli K12. Production of an active homoserine dehydrogenase fragment.
Open Access
- 1 November 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (21), 7685-7689
- https://doi.org/10.1016/s0021-9258(17)41022-2
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- Subunit Structure of the Methionine‐Repressible Aspartokinase II–Homoserine Dehydrogenase II from Escherichia coli K12European Journal of Biochemistry, 1977
- X-Ray Studies of Protein InteractionsAnnual Review of Biochemistry, 1974
- Cytochrome b2 from Bakers' Yeast (L‐Lactate Dehydrogenase)European Journal of Biochemistry, 1974
- The Threonine‐Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12European Journal of Biochemistry, 1973
- Nucleation, Rapid Folding, and Globular Intrachain Regions in ProteinsProceedings of the National Academy of Sciences, 1973
- The Threonine‐Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K12European Journal of Biochemistry, 1972
- Proteolytic Cleavage of Native DNA Polymerase into Two Different Catalytic FragmentsEuropean Journal of Biochemistry, 1971
- Tertiary structure of Escherichia coli β-d-galactosidaseJournal of Molecular Biology, 1969
- Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gelsBiochemical and Biophysical Research Communications, 1967
- Regulation by methionine of the synthesis of third aspartokinase and of a second homoserine dehydrohenase in Escherichia coli K 12Biochimica et Biophysica Acta (BBA) - General Subjects, 1967