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Title: Characterization and function of stentorin, the photoreceptor protein in Stentor coeruleus

Thesis/Dissertation ·
OSTI ID:7191680

Stentorin is a photoreceptor protein that is responsible for the step-up photophobic response and the negative phototaxis of an aneural unicellular ciliate protozoan, Stentor coeruleus. This protein was solubilized from the membrane of pigment granules and purified by the combination of gel filtration, hydroxylapatite chromatography, and DEAE-sepharose anionic exchange chromatography. SDS polyacrylamide gel electrophoresis revealed two red fluorescent bands for the purified stentorin reflecting the microheterogeneity of stentorin. The fluorescence lifetime study of stentorin employing the deuterium solvent isotope effect was conducted to confirm the proton dissociation from the chromophore at the excited state as a primary signal in the photosensory transduction in S. coeruleus. The increase of the amplitude of the anionic lifetime component in going from H/sub 2/O buffer to D/sub 2/O buffer is suggestive of the existence of the conjugate acid-base network of the photoreceptor protein for fast proton transfer. ATP-involvement in the photoresponse of S. coeruleus was investigated by using the firefly bioluminescence for ATP assay and the incorporation of /sup 32/Pi into ATP. Light-induced ATP level variation was detected only when cellular ATP was extracted by the boiling water method. The cellular ATP level was constant regardless of light illumination when extracted by trichloroacetic acid (TCA).

Research Organization:
Texas Tech Univ., Lubbock (USA)
OSTI ID:
7191680
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English