THE α-CHYMOTRYPSIN EFFECT ON VARIOUS 9-AMINOACRIDINE FLUORESCENT PROBE EMISSION
| Autor: | Alain Marty, Madeleine Bourdeaux, Monique Dell' Amico, Pierre Viallet |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Binding Sites
Quenching (fluorescence) Chymotrypsin biology Aminoacridines Stereochemistry Tryptophan Active site General Medicine Biochemistry Fluorescence Fluorescence spectroscopy Kinetics Structure-Activity Relationship chemistry.chemical_compound Bimolecular fluorescence complementation Spectrometry Fluorescence chemistry Aromatic amino acids biology.protein Biophysics Physical and Theoretical Chemistry Protein Binding |
| Zdroj: | Photochemistry and Photobiology. 40:175-183 |
| ISSN: | 0031-8655 |
| DOI: | 10.1111/j.1751-1097.1984.tb04572.x |
| Popis: | The influence of a-chymotrypsin upon the fluorescence of various 9-aminoacridine derivatives was examined. Fluorescence is quenched in the presence of this protein. Moreover, quenching is suppressed by the coexistence of hydrocinnamic acid, a competitive inhibitor of the enzyme activity. This leads us to conclude that there is a fluorescent complex formation between protein and fluorophores. Then, the apparent association constants were calculated and the florescence lifetimes of “free” and “bound” 9-aminoacridine were determined by phase-modulation fluorometry. It is deduced that 9-aminoacridine compounds are probably located in the enzymatic active site and that the fluorescence quenching is not due to specific interactions with amino acid residues but is a consequence of the characteristics of this binding site, in particular its hydrophobicity and polarity. Alternatively, when these fluorescent probes are located in the vicinity of some aromatic amino acids (histidin, tryptophan and tyrosin), then the production of non fluorescent complex takes place. It is concluded that 9-aminoacridine compounds can be used for the determination of the type of amino acid residues in the binding sites of proteins. |
| Databáze: | OpenAIRE |
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