A new (G)γ-globin variant causing low oxygen affinity: Hb F-Brugine/Feldkirch [(G)γ105(G7)Leu→His; HBG2: c.317T>A]

Hemoglobin. 2014;38(2):84-7. doi: 10.3109/03630269.2013.870079. Epub 2014 Feb 7.

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.

Publication types

  • Case Reports

MeSH terms

  • Base Sequence
  • Binding, Competitive
  • Chromatography, High Pressure Liquid
  • Cyanosis / genetics
  • Cyanosis / metabolism
  • DNA Mutational Analysis
  • Female
  • Fetal Hemoglobin / genetics*
  • Fetal Hemoglobin / metabolism
  • Hemoglobins, Abnormal / genetics*
  • Hemoglobins, Abnormal / metabolism
  • Histidine / genetics
  • Humans
  • Infant, Newborn
  • Leucine / genetics
  • Male
  • Mutation, Missense*
  • Oxygen / metabolism*
  • Protein Binding
  • gamma-Globins / genetics*
  • gamma-Globins / metabolism

Substances

  • Hemoglobins, Abnormal
  • gamma-Globins
  • hemoglobin F-Brugine Feldkirch
  • Histidine
  • Fetal Hemoglobin
  • Leucine
  • Oxygen