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Hb J Taichung is the second singly-fast variant to be found among Chinese residents of Taiwan. The increased electrophoretic mobility of this hemoglobin results from the replacement in the β-chain of an alanyl residue by an aspartyl residue at the β-129 or βH7 position. Hb J Meinung, which was reported previously in Chinese subjects in Taiwan, has its structural aberration at β-56 or βD7 position where aspartyl replaces the glycyl residue normally found at that location. Hb J Taichung and Hb A occurred in the proportions of 41–59 in the one subject studied thus far. Although no detailed hematological study has been made, the subject appears to be normal with no obvious signs of anemia.

Hb J Kaohsiung was found, in 1969, in one Taiwanese male resident of Kaohsiung City, Taiwan, during a population survey for hemoglobin variants. From the results of the present chemical structural analyses it is concluded that the site of the anomaly in this singly-fast variant is the β-59 or βE 3 position where a threonyl group replaces the lysyl group normally present. From the chromatographic separations of the mixture of Hb A/J using a DEAE Sephadex column it was found that the relative amounts of Hb A 0 and Hb J Kaohsiung were 53 and 47%, respectively. Hb J Kaohsiung represents the third singly-fast or J-type hemoglobin variant found thus far in Chinese subjects in Taiwan. Previously, Hb J Meinung and Hb J Taichung were reported to have the respective anomalies of β56 (βD7) Gly → Asp and β129 (βH 7 ) Ala → Asp.