Linear dichroism studies of tryptophanase and its quasisubstrate complexes oriented in polyacrylamide gel
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1990.tb19329.x/fullpdf
Reference36 articles.
1. Substrate-protein interaction in tryptophanase from Bacillus alvei. Kinetic and spectral evaluations.
2. Monovalent cation activation of tryptophanase.
3. 4. Yu. M. Torchinsky, I. S. Sakharova, L. N. Zakomirdina, P. Christen, and T. Korpela (1987 ) inBiochemistry of vitamin B6() pp.233 -237 , Birkhauser Verlag, Basel.
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2. Crystals of Tryptophan Indole-Lyase and Tyrosine Phenol-Lyase Form Stable Quinonoid Complexes;Journal of Biological Chemistry;2002-06
3. Interactions of Escherichia coli tryptophanase with quasisubstrates and monovalent cations studied by the circular dichroism and fluorescence methods;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1996-05
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5. [10] Linear dichroism;Metallobiochemistry Part C: Spectroscopic and Physical Methods for Probing Metal Ion Environments in Metalloenzymes and Metalloproteins;1993
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