Primary Structure of Hopkins–I Haemoglobin

Abstract

HopKiNS–1 haemoglobin (haemoglobin Ho–1) was originally described in twelve members of a large kindred in 1958 by Smith and Torbert¹. In this investigation the abnormal haemoglobin was estimated to make up about 50 per cent of the total haemoglobin in affected heterozygotes. Although the β chain has been established as the site of amino-acid substitution by the recombination of haemoglobin sub-units², the nature and exact locus of the substitution have not yet been elucidated. Because haemoglobin Ho–1 is of the rapidly migrating haemoglobin I type electrophoretically, and therefore differs from haemoglobin A by two charges per abnormal chain, it can therefore be presumed that the mutation in haemoglobin Ho–1 involves the substitution of an acidic for a basic amino-acid.