Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Homogeneous complexes of bacteriorhodopsin (BR) from Halobacterium halobium purple membrane (PM) and 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) have been produced by a detergent-free process in which bovine liver non-specific phospholipid transfer protein (nsTP) promotes net transfer of DMPC from small unilamellar vesicles directly into PM. The number of DMPC molecules incorporated per BR monomer follows a close to linear dependence with the relative proportions of DMPC and PM added to the initial mixture over the ranges studied. The resulting complexes, with total lipid phosphate/BR contents of between 31:1 and 152:1 (mole/mole), were purified free from any remaining unincorporated DMPC by sucrose density gradient centrifugation. Broad line 31P-NMR spectra and partitioning studies with the nitroxide spin label, Tempo, confirm that the BR and DMPC coexist in bilayer complexes. Quantitative analysis of high resolution 31P-NMR spectra from complexes after solubilization in 4% SDS revealed 74-84% of the major PM phospholipid to be retained in the complexes.


Journal article


Biochem Biophys Res Commun

Publication Date





939 - 944


Animals, Bacteriorhodopsins, Carrier Proteins, Cattle, Dimyristoylphosphatidylcholine, Halobacterium, Lipid Bilayers, Liposomes, Liver, Magnetic Resonance Spectroscopy, Membrane Proteins, Molecular Conformation, Phospholipid Transfer Proteins, Protein Conformation, Thermodynamics