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Fig. 5 | Parasites & Vectors

Fig. 5

From: Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, Dioctophyme renale

Fig. 5

Hydrophobic ligand-binding by D. renale P44. a Superdex 75-purified and delipidated P44 (1.3 μM) was added to the non-specific hydrophobic probe ANS (3.3 μM) in PBS causing a dramatic increase in the probe’s fluorescence emission. Successive additions of 0.5 μl of 1 mM oleic acid partially reversed the fluorescence enhancement. Excitation wavelength = 350 nm. b P44 (1.3 μM) added to the dansyl fluorophore-tagged fatty acid DAUDA (0.3 μM) in buffer yielding a dramatic increase in fluorescence intensity and blue shift in DAUDA’s peak wavelength of emission from 544 nm to 470 nm. This was reversed with successive additions of 0.5 μl of 1 mM oleic acid solution. Similar experiments using D. renale P17 revealed no binding of DAUDA (not shown). Excitation wavelength = 345 nm. c Intrinsic (predominantly tryptophan) protein fluorescence emission by P44. P44 in buffer was excited at 295 nm producing peak fluorescence emission at 338 nm. Successive additions of 0.5 μl of 1 mM oleic acid solution in ethanol to 300 μl protein in PBS produced only very slight if any changes in emission intensity and wavelength of peak emission. The spectrum of buffer alone (shown) was subtracted from each of the P44 intrinsic fluorescence emission spectra

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