Rapid differentiation of polypeptide chains of hemoglobin by cellulose acetate electrophoresis of hemolylsates.

The solubility of 14 hybrid haemoglobins composed of α chains with a single substitution and β chains from HbS was compared with that of sickle haemoglobin. A substantial reduction in the insolubility of native deoxyhaemoglobin S results from surface mutations in certain regions of the α chain while changes in other areas have no effect. Also, the chemical nature of the substitution is decisive and points to the type of intermolecular bonding at several loci.

Location and bond type of intermolecular contacts in the polymerisation of haemoglobin S

alpha Chain mutations with opposite effects on the gelation of hemoglobin S.

We describe a method of electrophoresis of hemoglobin on cellulose acetate plates impregnated with citrate agar, which remain stable for many months and are used to confirm rapidly the presence of hemoglobins S and C and the hemoglobinopathies associated with them. The method also provides excellent separations of hemoglobins F and A and reliable identification of genetically determined hemoglobin abnormalities in the newborn.

Identification of hemoglobins and hemoglobinopathies by electrophoresis on cellulose acetate plates impregnated with citrate agar.

Five new double-mutant haemoglobins composed of betaS chains and alpha chains with different substitutions, which are located at the surface of the tetramer, have been prepared. Although all the hybrids are more soluble than deoxyhaemoglobin S, the individual differences between these molecules make it possible to evaluate several regions on the alpha chains for intermolecular contacts in the polymerisation of deoxyhaemoglobin S.

S. Ueda

Papers

Hemoglobin sealy (alpha 2-47His-beta 2): a new variant in a Jewish family.

Hemoglobin Sealy (α247Hisβ2): a new variant in a Jewish family.