6533b86efe1ef96bd12cbc26

RESEARCH PRODUCT

Time-dependent monomerization of bacteriorhodopsin in triton X-100 solutions analyzed by high-performance liquid chromatography

Thomas NawrothRainer PabstKlaus Dose

subject

Liposomefood.ingredientChromatographybiologyOrganic ChemistryPhotoproteinBacteriorhodopsinGeneral Medicinebiology.organism_classificationBiochemistryHigh-performance liquid chromatographyLecithinAnalytical Chemistrychemistry.chemical_compoundfoodchemistrybiological sciencesTriton X-100biology.proteinNative stateHalobacteriaceae

description

Abstract Bacteriorhodopsin from Halobacterium halobium was monomerized in Triton X-100 solutions. The process of delipidation was monitored by size-exclusion high-performance liquid chromatography under conditions that preserved the native conformation of the protein. The effects on the process of monomerization of the concentration and pH of the Triton X-100 solutions were investigated. The monomeric bacteriorhodopsin separated was active in light-dependent proton translocation when incorporated into soy bean lecithin liposomes.

yearjournalcountryeditionlanguage
1984-01-01Journal of Chromatography A
https://doi.org/10.1016/s0021-9673(01)87774-8