Novel instrumentation and biomedical applications of very near infrared fluorescence
| Autor: | Marc B. Brown, Nichola J. Seare, David P. Riley, Tony E. Edmonds, James Miller |
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| Rok vydání: | 1993 |
| Předmět: |
Instrumentation
Fluorescence spectrometry Analytical chemistry Lactoglobulins Ovomucin Biochemistry Analytical Chemistry chemistry.chemical_compound Oxazines Electrochemistry medicine Environmental Chemistry Bovine serum albumin Spectroscopy Fluorescent Dyes chemistry.chemical_classification Binding Sites biology Nile red Serum Albumin Bovine Blood Proteins Orosomucoid Propranolol Fluorescence Flufenamic Acid Wavelength Spectrometry Fluorescence Flufenamic acid chemistry biology.protein Biophysics Glycoprotein medicine.drug |
| Zdroj: | The Analyst. 118:407 |
| ISSN: | 1364-5528 0003-2654 |
| DOI: | 10.1039/an9931800407 |
| Popis: | A high wavelength fluorescent probe, Nile Red, was added to four proteins, viz., bovine albumin, alpha 1-acid glycoprotein, beta-lactoglobulin and ovomucoid. Nile Red showed an enhancement in fluorescence and a shift in emission wavelength, suggesting it was bonding hydrophobically to these proteins. Drug displacement of Nile Red from alpha 1-acid glycoprotein was achieved with both D,L-propranolol and flufenamic acid, showing that the binding site is less electrostatic and more hydrophobic in nature. In order to monitor these interactions, a simple spectrofluorimeter was constructed from solid-state components; the sensitivity of this instrument compared well with that of standard laboratory spectrofluorimeters. |
| Databáze: | OpenAIRE |
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