title: Purification of an LHI-RC-complex of Rhodospirillum rubrum by solubilization of chromatophores with a short-chain lecithin.
abstract: Chromatophores from Rhodospirillum rubrum were solubilized using the detergent 1,2-diheptanoyl-sn-phosphatidylcholine (DHPC). The solubilization curves are sigmoidal reaching a plateau at a detergent/protein ratio of 2-3 μmol/mg corresponding to 75-90% solubilized protein. The BChl-binding proteins are stable over a large range of DHPC/protein ratios. A complex of BChl-binding proteins containing both LHI- and RC-polypeptides (LHI-RC-complex) was purified using a two step procedure. RC photochemical activity as well as absorption and near-IR CD spectra showed the complex to be active and stable after purification in presence of DHPC.
authors.affiliation: Institute of Plant Biology, University of Zürich, Zollikerstrasse 107, CH-8008, Zürich, Switzerland.
authors.forename: J
authors.initials: J
authors.lastname: Kessi
authors.forename: R
authors.initials: R
authors.lastname: Ghosh
authors.forename: R
authors.initials: R
authors.lastname: Bachofen