Literature DB >> 7055530

The IgG binding function of the normal red cell plasma membrane: identification of integral polypeptides that bind IgG.

E J Victoria, L C Mahan, S P Masouredis.   

Abstract

Non-immune IgG binds to red cell integral membrane proteins obtained by mild alkaline extraction of ghosts. Detergent gel chromatography and electrophoretic analyses of IgG-membrane protein complexes obtained by nonionic detergent solubilization and affinity binding to protein A indicate that three polypeptides participate in the binding of IgG. These have apparent molecular weights of 90 000, 44 000 and 22 000 and are present in a 1:3:0.9 stoichiometry. Evidence obtained indicates that the major sialoglycoproteins are not involved in this type of binding.

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Year:  1982        PMID: 7055530     DOI: 10.1111/j.1365-2141.1982.tb01895.x

Source DB:  PubMed          Journal:  Br J Haematol        ISSN: 0007-1048            Impact factor:   6.998


  3 in total

1.  Naturally occurring anti-band 3 antibodies in clearance of senescent and oxidatively stressed human red blood cells.

Authors:  Hans U Lutz
Journal:  Transfus Med Hemother       Date:  2012-08-27       Impact factor: 3.747

Review 2.  Antigenicity, storage, and aging: physiologic autoantibodies to cell membrane and serum proteins and the senescent cell antigen.

Authors:  M M Kay; K Sorensen; P Wong; P Bolton
Journal:  Mol Cell Biochem       Date:  1982-11-26       Impact factor: 3.396

3.  Non-immune interaction of erythrophilic IgG fractions with human red blood cells.

Authors:  S Dagan; A Beretz; M Fridkin; Y Burstein; Z Spirer
Journal:  Mol Cell Biochem       Date:  1985-02       Impact factor: 3.396

  3 in total

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