Interaction of beta zero thalassemia with Hb San Diego [a high affinity hemoglobin variant, alpha 2 beta (2)109(G11)Val----Met] in a 29-year-old Greek male is described. A marked polycythemia with low MCH and MCV, but minor clinical problems were observed. Functional properties of the isolated variant are described.

A 26-year-old French woman born in Saverne (France) was found to have Heinz body hemolytic anemia. Isoelectrofocusing showed the presence of an abnormal band amounting to 35% of the total hemoglobin concentration, suggesting a beta variant. Structural analysis of the abnormal beta chain showed an elongated C-terminal segment. Histidine 143 is replaced by a proline and the C-terminal sequence is identical to the corresponding segment of Hb Cranston. This new variant, named Hb Saverne, has beta chains composed of 156 amino acid residues. Studies of its functional properties showed that Hb Saverne is an unstable, high affinity variant with low cooperativity.

While investigating the mechanism of a beta-thalassemia intermedia phenotype in a 34 year old Thai male, a new Hb variant beta 126 Val----Gly named Hb Dhonburi was discovered. Genetic and structural studies revealed the existence of a beta zero-thalassemia genotype in association with the beta variant. The new variant is unstable but exhibits normal oxygen binding properties. Hb Dhonburi was also discovered in the mother of the propositus in association with Hb E.

A new abnormal hemoglobin was found in a diabetic Maltese woman by citrate agar electrophoresis. This variant was undetectable by isoelectric focusing. No hematological abnormalities were observed. The structural analysis included isolation of the abnormal b chain, high pressure liquid chromatography of the corresponding tryptic peptides and then microsequencing of the abnormal T,. These procedures revealed a double abnormality: the presence of a methionyl residue extending the NH, terminus and a histidine to proline substitution in position NA,. Hemoglobinopathy /I variant HPLC