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Hemoglobin Lyon-Bron was found in two members of a family of German ascent presenting with a moderate normocytic anemia. In this alpha2 globin variant, the N-terminal valine of the chain was replaced by an alanine. Electrospray mass spectrometry of the α chain showed that, as normally, the initiator methionine was cleaved during globin processing but that the Nα-terminal group was totally acetylated. This resulted in structural modifications of a region crucial for oxygen binding. As a consequence, hemoglobin Lyon-Bron displayed both a reduced chloride effect and a decreased oxygen affinity, this last point explaining the apparent anemia. Am. J. Hematol. 69:214–218, 2002. © 2002 Wiley-Liss, Inc.

Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro) is a new unstable variant, with high oxygen affinity responsible, in the steady state, for an apparently well-compensated chronic hemolytic anemia. The functional properties of this variant are due to the replacement of a leucine residue which is involved in the hydrophobic environment of the proximal side of the heme. This electrophoretically neutral hemoglobin was found as a de novo case in a 6-year-old girl suffering from severe anemia with hemolysis and transient aplastic crisis, following infection by parvovirus B19.