title: Lipid composition and proton transport in Penicillium cyclopium and Ustilago maydis plasma membrane vesicles isolated by two-phase partitioning.
abstract: Plasma membranes have been isolated and purified from two species of fungi, Penicillium cyclopium and Ustilago maydis, using a two-phase aqueous polymer technique. The membranes were characterised using marker enzyme assays (e.g., vanadate-sensitive (Mg(2+)-K+)-ATPase and glucan synthetase II) and lipid composition (sterol enrichment, increased phosphatidylethanolamine/phosphatidylcholine ratio, and the absence of diphosphatidylglycerol). The proton-pumping activities of the plasma membrane-bound H(+)-ATPases from these species were compared. H(+)-ATPase activity was found to be greater in U. maydis than in P. cyclopium, which was attributed to differences in orientation of the plasma membrane vesicles. There was evidence to suggest the presence of redox chain activity in the plasma membranes of both species.
authors.affiliation: Department of Agricultural Sciencies, University of Bristol, UK.
authors.forename: A
authors.initials: A
authors.lastname: Hernández
authors.forename: D T
authors.initials: DT
authors.lastname: Cooke
authors.forename: D T
authors.initials: DT
authors.lastname: Clarkson
mesh_terms: D002458:Cell Fractionation / Q000379:methods; D002462:Cell Membrane / Q000737:chemistry; D004875:Ergosterol / Q000032:analysis; D008055:Lipids / Q000032:analysis*; D010084:Oxidation-Reduction; D010407:Penicillium / Q000737:chemistry* / Q000201:enzymology; D017494:Proton Pumps / Q000032:analysis; D006180:Proton-Translocating ATPases / Q000032:analysis* / Q000037:antagonists & inhibitors; D014588:Ustilago / Q000737:chemistry* / Q000201:enzymology
chemical_list: D008055:Lipids; D017494:Proton Pumps; D006180:Proton-Translocating ATPases; D004875:Ergosterol