Tryptophan synthase of Escherichia coli. Removal of pyridoxal 5'-phosphate and separation of the alpha and beta2 subunits.
Open Access
- 1 October 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (19) , 6594-6599
- https://doi.org/10.1016/s0021-9258(17)39889-7
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Cooperative and noncooperative binding of pyridoxal 5'-phosphate to tryptophan synthase from Escherichia coliBiochemistry, 1976
- Effects of salts on the subunit structure and dissociation of Lumbricus terrestris hemoglobinBiochemistry, 1975
- Effects of modification of the β2 subunit and of the α2β2 complex of tryptophan synthase by α-cyanoglycine, a substrate analogBiochemical and Biophysical Research Communications, 1975
- Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunitBiochemistry, 1970
- Association of β-chain monomers of Escherichia coli tryptophan synthetaseBiochemistry, 1970
- Ion effects on the solution structure of biological macromoleculesAccounts of Chemical Research, 1969
- A new thiol-dependent transamination reaction catalyzed by the B protein of Escherichia coli tryptophan synthetaseBiochemistry, 1968
- Subunit structure of the tryptophan synthetase of Escherichia coliJournal of Molecular Biology, 1966
- On the Role of Pyridoxal 5'-Phosphate in Phosphorylase. II. Resolution of Rabbit Muscle Phosphorylase b*Biochemistry, 1966
- A study of the catalytic properties of Escherichia coli tryptophan synthetase, a two-component enzymeArchives of Biochemistry and Biophysics, 1962