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Red Blood Cell

The main function is to deliver oxygen to the tissue and helps in the disposal of carbon dioxide and protons formed by tissue metabolism. Hemoglobin- about 95% of its intracellular protein There are no intracellular organelles such as mitochondria, lysosomes or Golgi apparatus. It is non-nucleated

 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.


about 50% lipid and 50% protein The major phospholipids are phosphatidyl choline, phosphatidyl ethanolamine, and phosphatidyl serine along with sphingomyelin. The Major Integral Proteins: Anion Exchange Protein & the Glycophorins Spectrin, Ankyrin, & Other Peripheral Membrane Proteins Help Determine the Shape & Flexibility of the Red Blood Cell


The anion exchange protein (band 3)

a transmembrane glycoprotein multipass membrane protein forms a tunnel, permitting the exchange of chloride for bicarbonate The amino terminal end binds many proteins, including hemoglobin, proteins 4.1 and 4.2, ankyrin, and several glycolytic enzymes.

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

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.

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


Biochemical basis of blood typing and of blood type determination.

Antibody Immune Response

H Substance Is the Biosynthetic Precursor of Both the A & B Substances

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

Roles of Genetics in determining the Blood type

Roles of Genetics in determining the Blood type

Predicting human blood types

What are the possible blood types of the offspring of a cross between individuals that are type AB and type O?

Cases on Blood Incompatibility

Hemolytic Disease of the Newborn

Hemolytic Disease of the Newborn

Erythroblastosis Fetalis Rh INCOMPATIBILITY- a condition which develops when a pregnant woman has an Rhnegative blood type and the fetus she carries has Rh-positive blood type.

Hemolytic Transfusion Reaction

blood transfused into an individual is an incompatible blood type may result to:
minor rise in the plasma bilirubin to severe jaundice renal tubular damage leading to death

Hemolytic Transfusion Reaction