Hemoglobin Gun Hill: deletion of five amino acid residues and impaired heme-globin binding.
Hemoglobin Gun Hill, a new variant of adult hemoglobin, was found in a Caucasian and one of his three daughters. The abnormal hemoglobin had only half of the expected number of heme groups. Five amino acid residues appeared to be missing from the beta-globin chains. These residues occur in linear sequence in normal beta-chains in a region involved in heme-globin binding. A deletion of five amino acids in the beta-chains of hemoglobin Gun Hill is postulated. The most likely mechanism for the origin of such a hemoglobin variant would appear to be unequal crossing-over during meiosis.
D000328:Adult; D000595:Amino Acid Sequence; D000755:Anemia, Sickle Cell; D001797:Blood Protein Electrophoresis; D005914:Globins / Q000032:analysis; D006455:Hemoglobins, Abnormal / Q000032:analysis*; D006801:Humans; D008297:Male; D008967:Molecular Biology; D010455:Peptides / Q000032:analysis*; D013789:Thalassemia; D014357:Trypsin
D006455:Hemoglobins, Abnormal; D010455:Peptides; D005914:Globins; D014357:Trypsin