edoc

Lipid environments in the yolk lipoprotein system : a spin-labeling study of the lipovitellin/phosvitin complex from Xenopus laevis

Birrell, G. B. and Anderson, P. B. and Jost, P. C. and Griffith, O. H. and Banaszak, L. J. and Seelig, J.. (1982) Lipid environments in the yolk lipoprotein system : a spin-labeling study of the lipovitellin/phosvitin complex from Xenopus laevis. Biochemistry, Vol. 21, H. 10. S. 2444-2452.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A5257522

Downloads: Statistics Overview

Abstract

Lipid/protein and lipid/lipid interactions in the yolk lipoprotein complex from Xenopus laevis were examined by introducing a series of lipid spin-labels into the complex and observing the electron spin resonance spectra as a function of the position of the label along the lipid chains, temperature, pH, and charge on the lipid polar head group. Analyses of the spectra show that, in addition to the expected component arising from lipid associated with protein, a second component with increased segmental flexibility and the greater temperature dependence characteristic of lipid/lipid interactions is observed. These spin-labeling data and supporting compositional data indicate that much of the lipid is organized into a lipid-rich region or pool, consistent with the earlier model derived from electron microscopy and diffraction data and with companion 31P and 2H nuclear magnetic resonance data reported in the preceding paper [Banaszak, L. J., & Seelig, J. (1982) Biochemistry (preceding paper in this issue)]. The bilayer-like component exhibits a greater restriction of motion compared to vesicles of the isolated lipids at the same temperature, as would be expected for a relatively small lipid pool. Phospholipids exchange between the two motionally distinguishable environments. The equilibrium binding undergoes a shift between these two environments as a function both of pH and of the charge on the phospholipid polar head group. This shift in average binding affinity is opposite in direction to that reported for membrane proteins and implicates negatively charged groups on the protein that repel negatively charged phospholipids. This effect is greatly reduced by alkaline phosphatase treatment, suggesting that some of the lipid binding sites are in close proximity to phosphorylated residues on the protein.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Biophysical Chemistry (Seelig J)
UniBasel Contributors:Seelig, Joachim
Item Type:Article, refereed
Bibsysno:Link to catalogue
Publisher:American Chemical Society
ISSN:0006-2960
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:18

Repository Staff Only: item control page