Purification of the yellow fluorescent protein from vibrio fischeri and identity of the flavin chromophore
A low molecular weight protein (∼ 25,000 D) exhibiting a yellow fluorescence emission peaking at ∼ 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 (λ max = 380, 460 nm) and th...
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Published in | Biochemical and biophysical research communications Vol. 146; no. 1; pp. 101 - 106 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
San Diego, CA
Elsevier Inc
15.07.1987
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | A low molecular weight protein (∼ 25,000 D) exhibiting a yellow fluorescence emission peaking at ∼ 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 (λ
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 (λ
max ∼ 495 nm), this protein induces a bright yellow luminescence (λ
max ∼ 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(87)90696-6 |