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Haemoglobin F Jamaica (α 2 γ 2 61 Lys→Glu; 136 Ala )
Author(s) -
Ahern Edgar J.,
Jones Richard T.,
Brimhall Bernadine,
Gray Robert H.
Publication year - 1970
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1970.tb01450.x
Subject(s) - polypeptide chain , residue (chemistry) , chain (unit) , electrophoresis , stereochemistry , chemistry , microbiology and biotechnology , amino acid , biology , biochemistry , physics , astronomy
S ummary . Two siblings of mixed Negro, East Indian and Caucasian parentage showed an abnormal haemoglobin component in infancy which had electrophoretic characteristics similar to Hb F Roma (Silvestroni & Bianco, 1963). The amino‐acid substitution responsible for the peculiar electrophoretic mobility was found to be in the gamma polypeptide chain (γ— 61(E5) Lys→Glu). The finding of an alanyl residue at position 136 of the γ‐chain of the abnormal component in the first born of these infants was repeated in the abnormal γ‐chain of the second infant. No functional abnormalities were found to be associated with this abnormal haemoglobin, which is designated Hb F Jamaica.