A chemical study of hemoglobin Norfolk.

In an English family living in the county of Norfolk, England, Ager, Lehmann, and Vella (2) have described the occurrence of an electrophoretically fast moving variant of human adult hemoglobin (hemoglobin A). This hemoglobin has been named hemoglobin Norfolk. Gammack et al. (3) have reported that hemoglobin Norfolk contains abnormal ac-peptide chains. By a microscale adaptation of the dissociation and reassociation method of Itano and Robinson (4), they were able to show formation of hemoglobin A (a#&*) from a mixture of hemoglobin S (o+&s) and of hemoglobin Norfolk ~~~~~~~~~~ /3@). Therefore, the @pept.ide chains of hemoglobin Norfolk are judged to be normal, and the abnormality must reside in the cr-peptide chains. The present paper reports an investigation of the chemical alteration of hemoglobin Norfolk and of the minor hemoglobin components present in the same individual. Only two abnormal human hemoglobins which are altered in the ar-peptide chain have so far been fully investigated: hemoglobin I (5) and hemoglobinGPhiladelphia. (6). 1 h n emo o m an aspartic acid residue gl b’ 1 has been found to substitute a lysine (5), and in hemoglobin GPhiladelphia a lysine takes the place of an asparagine residue (6).