High-molecular-weight viral DNAs have been packed into proteoliposomes prepared by reverse-phase evaporation followed by phospholipid membrane targeting by influenza virus glycoprotein bound to hydrophobic 'anchors'. DNA has been encapsulated in the form of spermine condensates--toroidal structures sized approx. 0.1 micron, resistant to ultrasound. The efficiency of entrapping into liposomes reached 30% for condensed DNA of Mr up to 3 X 10(7). Specific infectivity of simian virus 40 DNA and simian adenovirus DNA packed into such proteoliposomes was 50- to 100-fold higher than that shown by free DNA preparations under Ca.phosphate-precipitation conditions.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/0378-1119(88)90535-5 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Membrane protein isolation and structure determination in cell-derived membrane vesicles.
Proc Natl Acad Sci U S A
May 2023
Laboratory of Molecular Neurobiology and Biophysics, The Rockefeller University, New York, NY 10065.
Integral membrane protein structure determination traditionally requires extraction from cell membranes using detergents or polymers. Here, we describe the isolation and structure determination of proteins in membrane vesicles derived directly from cells. Structures of the ion channel Slo1 from total cell membranes and from cell plasma membranes were determined at 3.
View Article and Find Full Text PDFCurrent problems and future avenues in proteoliposome research.
Biochem Soc Trans
August 2020
Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland.
Membrane proteins (MPs) are the gatekeepers between different biological compartments separated by lipid bilayers. Being receptors, channels, transporters, or primary pumps, they fulfill a wide variety of cellular functions and their importance is reflected in the increasing number of drugs that target MPs. Functional studies of MPs within a native cellular context, however, is difficult due to the innate complexity of the densely packed membranes.
View Article and Find Full Text PDFKinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes.
Proc Natl Acad Sci U S A
February 2020
Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden;
Article Synopsis
- - Mitochondria's inner membrane has structures called cristae which are believed to help create local proton gradients necessary for ATP synthesis, but their exact role in energy conversion is unclear.
- - Research measured local pH levels in mitochondria of yeast cells and found that only minor proton gradients exist in both typical and cristae-less cells, leading to low ATP synthesis rates, despite adequate driving forces.
- - The study concludes that the inner membrane's structure doesn't impact pH levels needed for ATP production, suggesting that the close arrangement of oxidative phosphorylation complexes in the cristae enhances the connection between proton pumping and ATP synthesis.
Lipid shape determination of detergent solubilization in mixed-lipid liposomes.
Colloids Surf B Biointerfaces
March 2020
Department of Chemical and Biomolecular Engineering, University of Tennessee, Knoxville, 1512 Middle Dr, Knoxville, TN 37996, USA. Electronic address:
The effects of lipid charge and head group size on liposome partitioning by detergents is an important consideration for applications such as liposomal drug delivery or proteoliposome formation. Yet, the solubilization of mixed-lipid liposomes, those containing multiple types of lipids, by detergents has received insufficient attention. This study examines the incorporation into and subsequent dissolution of mixed-lipid liposomes comprised of both egg phosphatidylcholine (ePC) and egg phosphatidic acid (ePA) by the detergent Triton-X100 (TX).
View Article and Find Full Text PDFPurification and characterization of the colicin A immunity protein in detergent micelles.
Biochim Biophys Acta Biomembr
November 2017
Instituto Biofisika (CSIC, UPV/EHU), Parque Científico de la UPV/EHU, Barrio Sarriena s/n, 48940 Leioa, Bizkaia, Spain. Electronic address:
The immunity proteins against pore-forming colicins represent a family of integral membrane proteins that reside in the inner membrane of producing cells. Cai, the colicin A immunity protein, was characterized here in detergent micelles by circular dichroism (CD), size exclusion chromatography, chemical cross-linking, nuclear magnetic resonance (NMR) spectroscopy, cysteine accessibility, and colicin A binding in detergent micelles. Bile-salt derivatives induced extensive protein polymerization that precluded further investigation.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!