Literature DB >> 658056

Incorporation and asymmetric orientation of glycophorin in reconstituted protein-containing vesicles.

E J van Zoelen, A J Verkleij, R F Zwaal, L L van Deenen.   

Abstract

Glycophorin can be incorporated in lipid vesicles without the use of detergents [MacDonald, R.J. and MacDonald, R.C. (1975) J. Biol. Chem. 250, 9206-9214]. In this paper it has been shown that the protein spans the lipid bilayer in these vesicles. In addition it has been shown that the protein is oriented in an asymmetric way with 75-80% of its sugar residues directed to the outside of the vesicles. Freeze-fracturing electron microscopy suggests that the protein is present in a slightly aggregated form. Sonication of these recombinants leads to the formation of small glycophorin-containing vesicles, in which almost all sugar residues are directed to the outside.

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Year:  1978        PMID: 658056     DOI: 10.1111/j.1432-1033.1978.tb12337.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

Review 1.  Freeze-etching studies of B cell membranes: recent progress.

Authors:  K de Groot
Journal:  Surv Immunol Res       Date:  1984

2.  Inhibition of phagocytosis by erythrocyte membrane sialoglycoprotein on target liposomes.

Authors:  S Utsumi; H Shinomiya; J Minami; S Sonoda
Journal:  Immunology       Date:  1983-05       Impact factor: 7.397

3.  Lipid-protein interaction in the glycophorin-dipalmitoylphosphatidylcholine system: Raman spectroscopic investigation.

Authors:  T Taraschi; R Mendelsohn
Journal:  Proc Natl Acad Sci U S A       Date:  1980-05       Impact factor: 11.205

  3 in total

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