A 50-year-old Japanese female patient was found to have hemolytic anemia. Isoelectrofocusing of her hemolysate revealed two abnormal hemoglobin bands, one of which wasveryclose to the Hb A2band, and the other between the Hb A2and Hb F bands. CM-cellulose column chromatography of the globin prepared from the abnormal hemoglobin showed that the abnormal chain eluted faster than the normalβandδchains; theβXchain, however, did not separate from the normalβchain in urea cellulose acetate electrophoresis. An instability test of the patient's hemolysate revealed the presence of an unstable component. Structural analysis of the abnormal B chain indicated that the histidine residue atβ92(F8) was replaced by an asparagine or aspartic acid residue. DNA amplified by poly-merase chain reaction was sequenced by the dideoxy method. The nucleotide sequence of theβ92 codon wasAAC instead ofCAC, suggesting that the amino acid substitution corresponded to His→tAsn, which is the same as is found in Hb Redondo or∼92(F8)His→Asn→Asp.