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Hemoglobin Shimonoseki, discovered in western Japan in 1960, has been further characterized as a mutant with abnormal α-polypeptide chains on the basis of: (1) The presence of a minor hemoglobin component migrating cathodally at pH 8.6 to Hb A2, presumably α2Shσ2A2. (2) Hybridization studies. (3) Fingerprinting of isolated α-polypeptide chains. Hemoglobin Sh is characterized by the substitution of arginine for glutamine at residue 54 and can therefore be designated as α254Argβ2A.
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Hanada et al. (1964) studied this question.
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