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• W2168486543 startingPage "39565" @default.
• W2168486543 abstract "Abstract Rhodopsin (Rho) has been extracted in n-dodecyl β-d-maltoside (DM) from bovine retinal rod outer segments and purified to homogeneity by affinity chromatography on concanavalin A-Sepharose. Because chemical cross-linking of Rho and photoactivated Rho (Rho*) provided initial evidence for the oligomeric nature of the photoreceptor protein, we carried out a hydrodynamic characterization of the native and activated conformations of detergent-solubilized Rho. The molecular weights of the complexes between dark and photoexcited states of Rho and DM were determined by gel filtration chromatography on Sephacryl S-300, in the presence of 0.1% DM. Subtracting the size of the corresponding detergent micelles resulted in molecular masses of 78 kDa for native Rho and 76 kDa for Rho*. The measured content of 0.97 g of detergent/g of protein resulted in a calculated partial specific volume of 0.765 cm3/g for the protein-detergent complex and a molar mass of 64–65 kDa for the protein moiety. The sizes of Rho·DM and Rho*·DM complexes were also evaluated by sedimentation on 10–30% sucrose gradients, in the presence of 0.1% DM, and molecular masses of about 60 kDa were estimated for both the dark- and light-activated states of the photoreceptor protein. The size of Rho was determined to be 65,300 and 69,800 Da, respectively, when the purified Rho·DM complex was either chromatographed on Sephacryl S-300 or ultracentrifuged on sucrose gradients in the absence of DM. All these results were consistent with a dimeric quaternary structure for both conformations of Rho. Additionally, the functional integrity of the purified photoreceptor protein following gel filtration chromatography and ultracentrifugation was demonstrated by three criteria as follows: (i) its characteristic UV-visible absorption spectra, (ii) its capability to photoactivate transducin, and (iii) its ability to serve as a substrate for rhodopsin kinase." @default.
• W2168486543 created "2016-06-24" @default.
• W2168486543 creator A5020881497 @default.
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• W2168486543 creator A5056313483 @default.
• W2168486543 date "2004-09-01" @default.
• W2168486543 modified "2023-10-13" @default.
• W2168486543 title "The Hydrodynamic Properties of Dark- and Light-activated States of n-Dodecyl β-D-Maltoside-solubilized Bovine Rhodopsin Support the Dimeric Structure of Both Conformations" @default.
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• W2168486543 doi "https://doi.org/10.1074/jbc.m402446200" @default.
• W2168486543 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15258159" @default.
• W2168486543 hasPublicationYear "2004" @default.
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