Biomaterial Database

Hemoglobin Gun Hill: deletion of five amino acid residues and impaired heme-globin binding. 1967

T B Bradley, and R C Wohl, and R F Rieder

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.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D008967	Molecular Biology	A discipline concerned with studying biological phenomena in terms of the chemical and physical interactions of molecules.	Biochemical Genetics,Biology, Molecular,Genetics, Biochemical,Genetics, Molecular,Molecular Genetics,Biochemical Genetic,Genetic, Biochemical,Genetic, Molecular,Molecular Genetic
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D001797	Blood Protein Electrophoresis	Electrophoresis applied to BLOOD PROTEINS.	Hemoglobin Electrophoresis,Electrophoresis, Blood Protein,Electrophoresis, Hemoglobin,Protein Electrophoresis, Blood
D005914	Globins	A superfamily of proteins containing the globin fold which is composed of 6-8 alpha helices arranged in a characterstic HEME enclosing structure.	Globin
D006455	Hemoglobins, Abnormal	Hemoglobins characterized by structural alterations within the molecule. The alteration can be either absence, addition or substitution of one or more amino acids in the globin part of the molecule at selected positions in the polypeptide chains.	Abnormal Hemoglobins
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000328	Adult	A person having attained full growth or maturity. Adults are of 19 through 44 years of age. For a person between 19 and 24 years of age, YOUNG ADULT is available.	Adults
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000755	Anemia, Sickle Cell	A disease characterized by chronic hemolytic anemia, episodic painful crises, and pathologic involvement of many organs. It is the clinical expression of homozygosity for hemoglobin S.	Hemoglobin S Disease,HbS Disease,Sickle Cell Anemia,Sickle Cell Disease,Sickle Cell Disorders,Sickling Disorder Due to Hemoglobin S,Anemias, Sickle Cell,Cell Disease, Sickle,Cell Diseases, Sickle,Cell Disorder, Sickle,Cell Disorders, Sickle,Disease, Hemoglobin S,Hemoglobin S Diseases,Sickle Cell Anemias,Sickle Cell Diseases,Sickle Cell Disorder