Article
Altered membrane structure and surface potential in homozygous hemoglobin C erythrocytes.
PloS one - 8 Jun 2009
Tokumasu Fuyuki, Nardone Glenn A, Ostera Graciela R, Fairhurst Rick M, Beaudry Steven D, Hayakawa Eri, Dvorak James A
Abstract excerpt
BACKGROUND: Hemoglobin C differs from normal hemoglobin A by a glutamate-to-lysine substitution at position 6 of beta globin and is oxidatively unstable. Compared to homozygous AA erythrocytes, homozygous CC erythrocytes contain higher levels of membrane-associated hemichromes and more extensively clustered band 3 proteins. These findings suggest that CC erythrocytes have a different membrane matrix than AA...
Topics
- Detergents
- Electrochemistry
- Electrophoresis, Polyacrylamide Gel
- Erythrocytes
- Flow Cytometry
- Glutamates
- Hemoglobin C
- Homozygote
- Humans
- Lipids
- Lysine