Isolation and properties of the β A- and γ F-chain subunits from normal adult and foetal haemoglobins

Abstract

Procedures for the isolation of the β A - and γ F -chain haemoglobin subunits from normal adult and foetal haemoglobin respectively are described. Tryptic peptide analyses of both species show complete absence of α A -chain peptides and presence of the known β A - or γ F -chain peptides. Reaction of either species with isolated α A -chain subunits produces new species with the mobilities of normal adult or foetal haemoglobin respectively, at approximately the same rates as with naturally occurring Hb- β 4 F or Hb- γ 4 F . The β A -chain subunits have been characterized by their electrophoretic mobility in starch gel, rates of alkaline denaturation, absorption spectra and the γ F -chain subunits, also by their recombination with canine haemoglobin and sedimentation properties. They cannot be distinguished by any of these criteria from their naturally occurring counterparts, Hb- β 4 A and Hb- γ 4 F , respectively. It is concluded that the latter two species will form in vivo if more β A - and γ F -chains are produced than α A -chains.