| Literature DB >> 6861750 |
G Helynck, B Luu, J L Nussbaum, D Picken, G Skalidis, E Trifilieff, A Van Dorsselaer, P Seta, R Sandeaux, C Gavach, F Heitz, D Simon, G Spach.
Abstract
Proteolipid apoproteins have been isolated from a whole bovine brain homogenate by chloroform/methanol extraction, and fractionated by chromatography on modified (lipophilic) Sephadex, followed by ion-exchange chromatography on CM-Trisacryl. The various final, highly hydrophobic, fractions are homogeneous (sodium dodecyl sulfate/polyacrylamide gel electrophoresis). Transmembrane ion transfers were studied by 22Na + flux and electrical conductance measurements. Single channel events were observed at low protein concentrations, in particular with one of the final homogeneous apoproteolipids of molecular mass 24 kDa.Entities:
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Year: 1983 PMID： 6861750 DOI： 10.1111/j.1432-1033.1983.tb07518.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956