Abstract

The apoprotein of human erythrocyte membranes was covalently spin-labelled with nitroxide-maleimide and mixed anhydride labels, before and after removal of sialic acids. The e.s.r. spectra and pH-induced spectral changes were compared with the reported spectra of native membranes. Interactions between the apoprotein and other lipids were examined using lipids containing spin probes. Lysolecithin was shown to bind more strongly than other lipids to membrane apoprotein. This binding was compared with the binding of lysolecithin to bovine serum albumin and acid casein. The formation of a lipoprotein complex between positively charged sialic acid free apoprotein and negatively charged sonicated dispersions of membrane lipid in an aqueous medium was examined using spin labels and spin probes. The data demonstrate that both polar and apolar interactions between the lipid and protein are involved in stabilisation of the complex.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.