Detection of an unstable murine hemoglobin

3H-leucine was used in vitro to label newly synthesized adult alpha and beta globins in reticulocytes removed from normal (Hba-b/Hba-b;Hbb-s2/Hbb-s2 and alpha-thalassemic (Hba-b2(th)/Hba-b;Hbb-s2/Hbb-s2) mice. The ratio of synthesis of beta-s2major: beta-sminor globins was 71:29 in reticulocytes from normal mice and 55:45 in reticulocytes from alpha-thalassemic mice. The two beta-globins are structurally identical except for a Val----Glu substitution at position 60. Denaturation of these mouse hemoglobins in isopropanol indicated that the tetramer containing the beta-s2major globin is unstable.