Site-directed mutagenesis of aspartate aminotransferase from E. coli
- 1 November 1985
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 132 (3), 915-921
- https://doi.org/10.1016/0006-291x(85)91894-7
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Aspartate Aminotransferase of Escherichia coli: Nucleotide Sequence of the aspC Gene1The Journal of Biochemistry, 1985
- Hydrogen bonding and biological specificity analysed by protein engineeringNature, 1985
- The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: Sequence comparison with pig isoenzymesBiochemical and Biophysical Research Communications, 1984
- Probing the catalytic mechanism of yeast triose phosphate isomerase by site-specific mutagenesisBiochemical Society Transactions, 1984
- Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structureJournal of Molecular Biology, 1984
- Directed Mutagenesis of Dihydrofolate ReductaseScience, 1983
- Efficient site-directed mutagenesis by simultaneous use of two primersNucleic Acids Research, 1983
- Primary structure of theompFgene that codes for a major outer membrane protein ofEscherichia coliK-12Nucleic Acids Research, 1982
- A rapid boiling method for the preparation of bacterial plasmidsAnalytical Biochemistry, 1981
- A sensitive method for the detection of aspartate: 2-oxoglutarate aminotransferase activity on polyacrylamide gelsAnalytical Biochemistry, 1981