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

Journal of Biological Chemistry

Volumn 279, Issue 38, 2004, Pages 39565-39573

  Medina, Rafael ^a   Perdomo, Deisy ^a   Bubis, José ^a  

^a UNIVERSIDAD SIMÓN BOLÍVAR   (Venezuela)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CHROMATOGRAPHY; OLIGOMERS; PROTEINS; SEDIMENTATION; SUGAR (SUCROSE); ULTRAVIOLET RADIATION;

ABSORPTION SPECTRA; GEL FILTRATION; PHOTORECEPTOR PROTEINS; RHODOPSINS;

HYDRODYNAMICS;

CONCANAVALIN A; DETERGENT; DODECYL BETA DEXTRO MALTOSIDE; MALTOSE; RHODOPSIN; RHODOPSIN KINASE; SEPHAROSE; TRANSDUCIN; UNCLASSIFIED DRUG; VISUAL PIGMENT;

AFFINITY CHROMATOGRAPHY; ANIMAL TISSUE; ARTICLE; CATTLE; COMPLEX FORMATION; CONFORMATION; CONTROLLED STUDY; CROSS LINKING; DARKNESS; ENZYME SUBSTRATE; GEL FILTRATION CHROMATOGRAPHY; HYDRODYNAMICS; LIGHT; MICELLE; MOLECULAR DYNAMICS; MOLECULAR WEIGHT; NONHUMAN; PHOTORECEPTOR; PHOTOSTIMULATION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN ISOLATION; PROTEIN PURIFICATION; PROTEIN QUATERNARY STRUCTURE; RETINA ROD; SEDIMENTATION; ULTRACENTRIFUGATION; ULTRAVIOLET SPECTROSCOPY;

ANIMALS; CATTLE; CHROMATOGRAPHY, GEL; CROSS-LINKING REAGENTS; DARKNESS; DETERGENTS; DIMERIZATION; GLUCOSIDES; LIGHT; MODELS, CHEMICAL; PHOTOCHEMISTRY; PROTEIN STRUCTURE, QUATERNARY; RHODOPSIN; SOLUBILITY; SUCROSE; TEMPERATURE; ULTRACENTRIFUGATION;

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 4544235707     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M402446200     Document Type: Article

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