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Recently, Ishimoto, Kuwata and Shotake reported a polymerizing hemoglobin found in Japanese monkey (Macaca fuscata) (J. Anthropol. Soc. Nippon 83, 233-243 (1975)). They separated the variant hemoglobin by gel filtration and from finger print results and from the fact that beta-mercaptoethanol dissociates the polymer deduced the substitution of an amino acid(s) by cysteine in the betaT10 peptide. We have purified the variant hemoglobin by ion-exchange chromatography using carboxymethyl cellulose after the protection of the reactive thiol groups with cystamine, and purified the betaT10 peptide and demonstrated that the usual glycine at beta 83 (EF 7) is substituted in the variant hemoglobin by cysteine.
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