8-Anilino naphthalene sulfonate binding as a probe for conformational changes induced in glutamate dehydrogenase by regulatory reagents
| Autor: | K.Lemone Yielding, Wynelle D. Thompson |
|---|---|
| Rok vydání: | 1968 |
| Předmět: |
Stereochemistry
Biochemical Phenomena Biophysics Naphthalenes Biochemistry Fluorescence chemistry.chemical_compound Glutamate Dehydrogenase Leucine Animals Nucleotide Molecular Biology Diethylstilbestrol chemistry.chemical_classification Aniline Compounds Binding Sites Phenanthridine Adenine Nucleotides Glutamate dehydrogenase Hydrogen-Ion Concentration Phenanthrenes Protein tertiary structure Guanine Nucleotides Kinetics Zinc Sulfonate Enzyme chemistry Liver Cattle NAD+ kinase Sulfonic Acids |
| Zdroj: | Archives of biochemistry and biophysics. 126(2) |
| ISSN: | 0003-9861 |
| Popis: | 8-Anilinonaphthalene sulfonate binds to a limited number of sites on bovine glutamate dehydrogenase and exhibits a large increase in fluorescence with a shift in the emission peak. The enzyme-enhanced fluorescence of the dye is sensitive to changes in enzyme tertiary structure, thus serving as a useful “probe” to study structure transitions evoked by a variety of regulatory reagents. Using this technique, reagents previously known to affect the structure and activity of the enzyme may be shown to to result in different conformational states. In addition, such reagents as diethylstilbestrol, Zn ++ , and phenanthridine, which have been shown to require NAD + or NADH for maximum effect on the enzyme, influence fluorescence of the enzyme-dye mixture independent of the presence of the nucleotide. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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