Purification of the yellow fluorescent protein from vibrio fischeri and identity of the flavin chromophore
| Autor: | Sandro Ghisla, R. Buntic, Pio Colepicolo, P. Steinerstauch, Peter Macheroux, J. W. Hastings, K.U. Schmidt |
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| Rok vydání: | 1987 |
| Předmět: |
Yellow fluorescent protein
Flavin Mononucleotide Biophysics Flavin mononucleotide Cell Biology Flavin group Biology Chromophore Photochemistry Biochemistry Fluorescence Molecular Weight Viral Proteins chemistry.chemical_compound Spectrometry Fluorescence chemistry ddc:570 biology.protein Bioluminescence Luciferase Luminescence Molecular Biology Vibrio |
| Zdroj: | Biochemical and Biophysical Research Communications. 146:101-106 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(87)90696-6 |
| Popis: | A low molecular weight protein (approximately 25,000 D) exhibiting a yellow fluorescence emission peaking at approximately 540 nm was isolated from Vibrio fischeri (strain Y-1) and purified to apparent homogeneity. FMN is the chromophore, but it exhibits marked red shifts in both the absorption (lambda max = 380, 460 nm) and the fluorescence emission. When added to purified luciferase from the same strain, which itself catalyzes an emission of blue-green light (lambda max approximately 495 nm), this protein induces a bright yellow luminescence (lambda max approximately 540 nm); this corresponds to the emission of the Y-1 strain in vivo. This yellow bioluminescence emission is thus ascribed to the interaction of these two proteins, and to the excitation of the singlet FMN bound to this fluorescent protein. |
| Databáze: | OpenAIRE |
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