Characterization of a chemical abnormality in hemoglobin G.

The development of methods (3,4) for localizing the differences in the primary structure of the human hemoglobins has prompted a study of the differences between the structures of hemoglobins A, S, and G. Knowledge of the structural differences might give new insight into the genetic control of the structure of these hemoglobins (5, 6). The results of this study, which are presented here, indicate that hemoglobins A, S, and G have different amino-terminal sequences in their P-chains. These sequences are as follows: