title: A new (G)γ-globin variant causing low oxygen affinity: Hb F-Brugine/Feldkirch [(G)γ105(G7)Leu→His; HBG2: c.317T>A].
abstract: In two unrelated families, several newborns developed cyanosis within the first days of life. For all of them, consecutive arterial blood gas analyses showed a right shift of the saturation curve, suggesting the presence of a hemoglobin (Hb) variant. A new (G)γ-globin variant was detected, namely (G)γ105(G7)Leu → His; HBG2: c.317T > A, that we named Hb F-Brugine/Feldkirch after the place of origin of the two families. This T to A conversion results in a leucine to histidine amino acid change at codon 105 of the (G)γ-globin gene and caused a Hb variant with lowered oxygen affinity. The γ to β switch proceeded normally.
authors: Institute for Medical & Molecular Diagnostics Ltd. , Zürich , Switzerland .
authors: Elisabeth
authors: E
authors: Saller
authors: Elisabeth
authors: E
authors: Kohne
authors: Fabrizio
authors: F
authors: Dutly
authors: Hannes
authors: H
authors: Frischknecht
mesh_terms: D001483:Base Sequence; D001667:Binding, Competitive; D002851:Chromatography, High Pressure Liquid; D003490:Cyanosis / Q000235:genetics / Q000378:metabolism; D004252:DNA Mutational Analysis; D005260:Female; D005319:Fetal Hemoglobin / Q000235:genetics* / Q000378:metabolism; D006455:Hemoglobins, Abnormal / Q000235:genetics* / Q000378:metabolism; D006639:Histidine / Q000235:genetics; D006801:Humans; D007231:Infant, Newborn; D007930:Leucine / Q000235:genetics; D008297:Male; D020125:Mutation, Missense; D010100:Oxygen / Q000378:metabolism*; D011485:Protein Binding; D055545:gamma-Globins / Q000235:genetics* / Q000378:metabolism
chemical_list: D006455:Hemoglobins, Abnormal; D055545:gamma-Globins; C000593191:hemoglobin F-Brugine Feldkirch; D006639:Histidine; D005319:Fetal Hemoglobin; D007930:Leucine; D010100:Oxygen