Plasma Membranes from Oats Prepared by Partition in an Aqueous Polymer Two-Phase System
Open Access
- 1 November 1982
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 70 (5), 1429-1435
- https://doi.org/10.1104/pp.70.5.1429
Abstract
Presumptive plasma membrane fractions have been prepared from oat (Avena sativa L. cv. Brighton) roots and shoots, respectively, by partition of microsomal fractions in a dextran-polyethylene glycol two-phase system. The plasma membranes had a high affinity for the polyethylene glycol-rich upper phase, whereas membranes from mitochondria and other organelles partitioned in the dextran-rich lower phase or at the interface. Thus, relatively pure plasma membranes were obtained by only two partition steps, and within 3 hours from homogenization of the material.Keywords
This publication has 17 references indexed in Scilit:
- Phase Partition—A Method for Purification and Analysis of Cell Organelles and Membrane VesiclesPublished by Wiley ,1982
- Blue light-induced Absorbance Changes in Membrane Fractions from Corn and NeurosporaPlant Physiology, 1977
- Auxin-binding Sites of Maize Coleoptiles Are Localized on Membranes of the Endoplasmic ReticulumPlant Physiology, 1977
- Isolation of Plasma Membranes from Corn Roots by Sucrose Density Gradient CentrifugationPlant Physiology, 1976
- β-Glucan Synthetases of Plasma Membrane and Golgi Apparatus from Onion StemPlant Physiology, 1974
- Purification of an Ion-Stimulated Adenosine Triphosphatase from Plant Roots: Association with Plasma MembranesProceedings of the National Academy of Sciences, 1972
- Characterization of three classes of chloroplasts obtained by counter-current distributionBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1971
- Correlation between Ion Fluxes and Ion-stimulated Adenosine Triphosphatase Activity of Plant RootsPlant Physiology, 1970
- Partition of Cell Particles and Macromolecules in Polymer Two-Phase SystemsAdvances in protein chemistry, 1970
- Tissue fractionation studies. 5. The association of acid phosphatase with a special class of cytoplasmic granules in rat liverBiochemical Journal, 1955