Hb taradale [beta82(EF6)Lys-->Arg]: a novel mutation at a 2,3-diphosphoglycerate binding site.
Hb Taradale [beta82(EF6)Lys-->Arg] was initially detected as a split Hb A0 peak on Hb A1c, monitoring. Red cell parameters, hemoglobin (Hb) electrophoresis and stability tests were normal. Mass spectrometry (ms) clearly identified a variant beta chain with a mass increase of 28 Da and peptide mapping located the mutation site to peptide betaT-9. DNA sequencing confirmed the presence of a novel beta82(EF6)Lys-->Arg mutation. This conservative substitution at a 2,3-diphosphoglycerate (2,3-DPG) binding site did not, however, appear to affect the P50 for oxygen binding.
Brennan
Stephen O
SO
Molecular Pathology Laboratory, Canterbury Health Laboratories, Christchurch, New Zealand. steve.brennan@chmeds.ac.nz
Sheen
Campbell
C
Chan
Tim
T
George
Peter M
PM
D019794:2,3-Diphosphoglycerate; D001665:Binding Sites; D004252:DNA Mutational Analysis; D006442:Glycated Hemoglobin / Q000032:analysis; D006455:Hemoglobins, Abnormal / Q000235:genetics*; D006801:Humans; D008297:Male; D013058:Mass Spectrometry; D008875:Middle Aged; D020125:Mutation, Missense; D010100:Oxygen / Q000378:metabolism
D019794:2,3-Diphosphoglycerate; D006442:Glycated Hemoglobin; D006455:Hemoglobins, Abnormal; D010100:Oxygen; C508161:hemoglobin Taradale