Products/Services Used | Details | Operation |
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Peptide Synthesis | Bovine rhodopsin was affinity- purified using the rhodopsin C-terminal antibody 1D4 (18) (University of British Columbia) coupled to Sepharose-4B (Sigma) and eluted using the nonapeptide (Genscript Limited, Hong Kong) corresponding to the C-terminal sequence of rhodopsin, the antibody epitope. | Get A Quote |
The chlorophyll-derivative chlorin e6 (Ce6) identified in the retinas of deep-sea ocean fish is proposed to play a functional role in red bioluminescence detection. Fluorescence and 1 H NMR spectroscopy studies with the bovine dim-light photoreceptor, rhodopsin, indicate that Ce6 weakly binds to it with μm affinity. Absorbance spectra prove that red light sensitivity enhancement is not brought about by a shift in the absorbance maximum of rhodopsin. 19 F NMR experiments with samples where 19 F labels are either placed at the cytoplasmic binding site or incorporated as fluorinated retinal indicate that the cytoplasmic domain is highly perturbed by binding, while little to no changes are detected near the retina... More