Location of three active site residues in the NH2-terminal sequence of the beta 2 subunit tryptophan synthase from Escherichia coli.
Open Access
- 1 January 1980
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 255 (2) , 512-517
- https://doi.org/10.1016/s0021-9258(19)86203-8
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Direct microsequence analysis of polypeptides using an improved sequenator, a nonprotein carrier (Polybrene), and high pressure liquid chromatographyBiochemistry, 1978
- Studies of the function and location of two cysteines in the β2 subunit of tryptophan synthaseBiochemical and Biophysical Research Communications, 1978
- Isolation and characterization of independently folding regions of the β chain of Escherichia coli tryptophan synthetaseBiochemistry, 1977
- Amino acid sequence of phospholipase A2-alpha from the venom of Crotalus adamanteus. A new classification of phospholipases A2 based upon structural determinants.Journal of Biological Chemistry, 1977
- Preparation and characterization of a modified form of beta2 subunit of Escherichia coli tryptophan synthetase suitable for investigating protein folding.Proceedings of the National Academy of Sciences, 1977
- Rapid analysis of amino acid phenylthiohydantoins by high-performance liquid chromatographyAnalytical Biochemistry, 1977
- Evidence that the essential, photosensitive histidyl residue in the β2 subunit of tryptophan synthetase is in the pyridoxyl peptideBiochemical and Biophysical Research Communications, 1974
- Advances in the gas chromatographic analysis of amino acid phenyl- and methylthiohydantoinsAnalytical Biochemistry, 1972
- Modification of methionyl residues during aminoethylationBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967
- [35] Detection of peptides by chemical methodsPublished by Elsevier ,1967