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Antigens Protected Functional Red Blood Cells By The Membrane Grafting Of Compact Hyperbranched Polyglycerols
11:31

Antigens Protected Functional Red Blood Cells By The Membrane Grafting Of Compact Hyperbranched Polyglycerols

Published on: January 2, 2013

The nature and abundance of human red cell surface glycoproteins

D J Anstee1

  • 1International Blood Group Reference Laboratory, South Western Regional Blood Transfusion Centre, Bristol, U.K.

Journal of Immunogenetics
|August 1, 1990
PubMed

Insights

Researchers identified a new red blood cell surface protein, Glycophorin E. A specific antibody, monoclonal anti-M, was found to detect this Glycophorin E product in typical red blood cells.

Area of Science:

  • Hematology
  • Molecular Biology
  • Immunology

Background:

  • Red blood cell surfaces possess at least 30 distinct proteins.
  • Protein abundance on red cells ranges widely, from hundreds to over a million copies per cell.
  • Recent advancements include the identification and sequencing of a novel Glycophorin gene, Glycophorin E.

Purpose of the Study:

  • To investigate the expression of the newly identified Glycophorin E gene product on normal red blood cells.
  • To determine if existing antibodies can detect the Glycophorin E protein.

Main Methods:

  • Utilized monoclonal antibody techniques.
  • Employed immunodetection methods to identify specific proteins on red blood cell surfaces.

Main Results:

  • Presented evidence that a monoclonal anti-M antibody recognizes the Glycophorin E gene product.
  • Confirmed the presence of Glycophorin E in normal red blood cells.

Conclusions:

  • Monoclonal anti-M serves as a reliable marker for detecting Glycophorin E.
  • This finding contributes to the understanding of red blood cell surface protein expression and characterization.

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