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Isolation of a prokaryotic photoreceptor: sensory rhodopsin from halobacteria
Author(s) -
Schegk E. Sebastian,
Oesterhelt Dieter
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb03151.x
Subject(s) - rhodopsin , size exclusion chromatography , biology , centrifugation , biochemistry , retinal , enzyme
The photoreceptor sensory rhodopsin was isolated from halobacterial cell membranes solubilized in laurylmaltoside. In the presence of retinal, detergent and salt the native protein was obtained in pure form by sucrose density gradient centrifugation, hydroxyapatite chromatography and gel filtration. The apparent mol. wt of the molecule was 24 kd if analysed by SDS gel electrophoresis, and 49 kd by sedimentation and size‐exclusion chromatographic analysis. The chromoprotein had an absorption maximum at 580 nm which was 8 nm blueshifted compared to the membrane‐bound state. The molecule was photochemically active and the action spectrum for formation of SR 380 , the long‐lived intermediate, coincided with the absorption spectrum.