title: Structural and functional studies of hemoglobin J Cala-bria: beta64 (E8) Gly leads to Asp.
abstract: A hemoglobin of high electrophoretic mobility was detected in a French male suffering from an acute leukemia; this hemoglobin was also present in his family. The variant was unstable and possessed an abnormal beta chain, in which a glycyl residue in position 64 (E8) was replaced by an aspartyl residue. This variant constitutes a new case of Hb J Calabria. Since the substituted E8 residue is in close spatial contact with that at B6, it was of interest to compare the properties of Hb J Calabria with those of other hemoglobins bearing substitutions at the same site.
mesh_terms: D000328:Adult; D000368:Aged; D000596:Amino Acids / Q000032:analysis; D001224:Aspartic Acid; D005260:Female; D005998:Glycine; D006448:Hemoglobin J / Q000502:physiology; D006455:Hemoglobins, Abnormal / Q000502:physiology; D006579:Heterozygote; D006801:Humans; D007525:Isoelectric Focusing; D007938:Leukemia / Q000097:blood*; D008297:Male; D010100:Oxygen / Q000097:blood; D010446:Peptide Fragments / Q000032:analysis
chemical_list: D000596:Amino Acids; D006455:Hemoglobins, Abnormal; D010446:Peptide Fragments; D001224:Aspartic Acid; D006448:Hemoglobin J; D010100:Oxygen; D005998:Glycine