8-Anilino naphthalene sulfonate binding as a probe for conformational changes induced in glutamate dehydrogenase by regulatory reagents
- 1 August 1968
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 126 (2), 399-406
- https://doi.org/10.1016/0003-9861(68)90424-4
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Interaction of glutamate dehydrogenase with fluorescent dyesBiochemical and Biophysical Research Communications, 1967
- Desensitization of the allosteric sites of glutamate dehydrogenase by fluorodinitrobenzeneBiochemical and Biophysical Research Communications, 1967
- Cooperative interaction between the GTP binding sites of glutamate dehydrogenaseBiochemical and Biophysical Research Communications, 1966
- The interaction of a naphthalene dye with apomyoglobin and apohemoglobinJournal of Molecular Biology, 1965
- Physicochemical properties of Bence-Jones proteins in the form of L-chain dimersBiochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1964
- Immunochemical evidence for multiple molecular forms of crystalline glutamic dehydrogenaseJournal of Molecular Biology, 1964
- Metal-ion requirement for pyridine nucleotide-induced disaggregation of glutamate dehydrogenaseBiochimica et Biophysica Acta, 1963
- Inhibition of glutamic dehydrogenase by o-phenanthroline and its analogsBiochimica et Biophysica Acta, 1962
- A Molecular probe for the antibody siteJournal of Molecular Biology, 1962
- The Binding of Organic Ions by Proteins1Journal of the American Chemical Society, 1946