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Cytosolic 3,3',5-tri-iodo-L-thyronine-binding proteins (CTBP I, II and IV species) from human red blood cells undergo rapid loss of activity at low temperatures. Cold treatment of CTBPs was accompanied by dissociation of the polymeric protein to the 60 kDa inactive monomer. Re-activation of the cold-inactivated CTBP IV by warming resulted in association of the monomer to the active polymeric form. A similar association-dissociation phenomenon was also obtained isothermically, though pH changes. We conclude that CTBP I and CTBP II are polymeric forms of CTBP IV.

biochemical journal

Molecular interconversion of cold-sensitive cytosolic 3,3′,5-tri-iodo-<scp>l</scp>-thyronine-binding proteins from human erythrocytes: effect of cold, heat and pH treatments

Molecular interconversion of cold-sensitive cytosolic 3,3′,5-tri-iodo-l-thyronine-binding proteins from human erythrocytes: effect of cold, heat and pH treatments