GROUP 4
ATP used is synthesized from Glycolysis and is important in processes that help the red cell maintain its biconcave shape and also in the regulation of the transport of ions.
Glycophorins A, B, and C
transmembrane glycoproteins but of the single-pass type A is the major glycophorin Glycophorin A contains binding sites for influenza virus and for Plasmodium falciparum
Spectrin
major protein of the cytoskeleton. It is composed of two polypeptides: spectrin 1 ( chain) and spectrin 2 ( chain). four binding sites can be defined in spectrin: (1) for self-association, (2) for ankyrin (bands 2.1, etc), (3) for actin (band 5), and (4) for protein 4.1.
Ankyrin
Pyramid-shaped protein that binds spectrin. It binds tightly to band 3, securing attachment of spectrin to the membrane. Ankyrin is sensitive to proteolysis
Actin (band 5)
short, double-helical filaments of F-actin. The tail end of spectrin dimers binds to actin. Actin also binds to protein 4.1.
Protein 4.1
a globular protein, binds tightly to the tail end of spectrin also binds to the integral proteins, glycophorins A and C, thereby attaching the ternary complex to the membrane may interact with certain membrane phospholipids, thus connecting the lipid bilayer to the cytoskeleton
Formed by Fucosyltransferase- that catalyses the addition of terminal fucose in alpha 1-> 2 linkage onto the terminal Gal residue of its precursor
The A Gene Encodes a GalNAc Transferase The B Gene a Gal Transferase The O Gene an Inactive Product
Importance of the oligosaccharide sequence in the RBC membrane in blood type determination
END OF REPORT.