Abnormal human hemoglobins IX. Chemistry of hemoglobin JBaltimore

Abstract

A human abnormal hemoglobin with the electrophoretic mobility of hemoglobin J has been isolated and studied. The amino acid substitution in this abnormal hemoglobin has been investigated. It has been found that an aspartic acid residue substitutes in this hemoglobin J the glycine residue present in position 16 of the β peptide chain. There are reasons to believe that the hemoglobin J studied is different from other hemoglobin J's. Accordingly, the hemoglobin studied has been specifically designated hemoglobin J_Baltimore.