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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© 1964 by American Society of Hematology, Inc.
1964
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