Description of Three New α Variants and Four New ß Variants: Hb Montluel [α110(G17)Ala → Val; HBA1: c.332C > T], Hb Cap d'Agde [α131(H14)Ser → Cys; HBA2: c.395C > G] and Hb Corsica [α100(G7)Leu → Pro; HBA1: 302T > C]; Hb Nîmes [ß104(G6)Arg → Gly; HBB: c.313A > G], Hb Saint Marcellin [ß112(G14)Cys → Gly; HBB: c.337T > G], Hb Saint Chamond [ß80(EF4)Asn → 0; HBB: c.241_243delAAC] and Hb Dompierre [ß29(B11)Gly → Arg; HBB: c.88G > C].

We present here seven new hemoglobin (Hb) variants identified during routine Hb analysis. All of them are caused by a missense mutation except Hb Saint Chamond, which results from an in-frame deletion of the asparagine residue at ß80. All these variants are clinically silent in the heterozygous state but two of them (Hb Cap d'Agde and Hb Dompierre) may be unstable, whereas Hb Nîmes could present a very slightly elevated oxygen affinity. These data are to be confirmed by appropriate biochemical tests.

A new hemoglobin variant: Hb Meylan [ß73(E17)Asp → Phe; HBB: c.220G>T; c.221A>T] with a double base mutation at the same codon.

We report a new ß-globin chain variant: Hb Meylan [ß73(E17)Asp → Phe; HBB: c.220G>T; c.221A>T]. The new variant results from a double nucleotide mutation at the same codon. The possible molecular mechanisms are discussed.