Abstract
Abstract— Spectral properties of guanidine‐denaturated and pronase‐digested green‐fluorescent proteins (GFP) from two species of bioluminescent coelenterates have been investigated. Spectrophotometric titrations of Renilla and Aequorea GFP, following denaturation in 6 M guanidine HCl at elevated temperature, revealed identical absorption peaks in acid (383–384 nm) and in alkali (447–448 nm) and a single isosbestic point in the visible region at 405 nm. Both proteins exhibited a spectrophotometric pK. of 8.1 in guanidine ‐HCl. Pronase digestion of the heat‐denaturated GFP's generated a methanol‐soluble blue‐fluorescent peptide with identical fluorescence emission spectra (λ max = 430 nm, uncorrected; φ f1 = 0.003) for both coelenterate species. These data suggest that the large absorption differences between native Renilla and Aequorea GFP molecules result from unique protein environments imported to a common chromophore.
Keywords
Aequorea victoriaFluorescenceChromophorePronaseChemistryGreen fluorescent proteinDenaturation (fissile materials)GuanidinePhotochemistryBiochemistryTrypsinNuclear chemistry
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Publication Info
- Year
- 1980
- Type
- article
- Volume
- 31
- Issue
- 6
- Pages
- 611-615
- Citations
- 205
- Access
- Closed
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William W. Ward,
Chris W. Cody,
Russell C. Hart
et al.
(1980).
SPECTROPHOTOMETRIC IDENTITY OF THE ENERGY TRANSFER CHROMOPHORES IN RENILLA AND AEQUOREA GREEN‐FLUORESCENT PROTEINS.
Photochemistry and Photobiology
, 31
(6)
, 611-615.
https://doi.org/10.1111/j.1751-1097.1980.tb03755.x
Identifiers
- DOI
- 10.1111/j.1751-1097.1980.tb03755.x