The authors presented the serum haptoglobin, a hereditary glycoprotein in the α
2 globulin fraction, as an example of a polymorphic system where different types react differently when subjected to unusual conditions. Naito, our collaborator, conducted an experiment in which various amounts of hemoglobin were administered intravascularly to young men of three different haptoglobin types, and demonstrated that when administration of an excess amount of hemolysate was given the patterns of production and clearance of Hb-Hp complex in individuals of Hp 2-2 were significantly different from those in individuals of Hp 2-1 or 1-1 (Naito, 1968). Such delicate individual differences in the gene-environment interaction have been more fundamentally demonstrated in normal and abnormal hemoglobins.
The principal material in the subsequent discussion is 21 kindreds with structural and synthetic abnormalities of the hemoglobin involving the α, β, γ and δ polypeptide chains, which have been studied by the First Department of Medicine, Kyushu University, since 1960. Among 18 structural abnormalities, 8 are hitherto undescribed ones.
View full abstract