Biomaterial Database

Antibodies to an NH2-terminal fragment of betaS globin. II. Specificity and isolation of antibodies for the sickle mutation. 1976

J G Curd, and N S Young, and A N Schechter

The immunochemical specificity of an antiserum produced to an NH2-terminal 55-residue polypeptide fragment of the betaS globin, betaS(1-55), was analyzed with a radioimmunoassay using the radioiodinated fragment as a tracer. These studies show that most of the antibodies have comparable reactivity with betaS(1-55), betaA(1-55), betaS globin, betaA globin, HbS, and HbA. However, the antiserum contains some antibodies which react only with the species derived from HbS. These "S" -specific antibodies were isolated by absorption of the serum on a column of betaA(1-55) coupled covalently to Sepharose. The S-specific antibodies have markedly diminished reaction with betaA(1-55) and HbA. The S specificity was localized to the valine substitution at position 6 of the beta globin, as shown by inhibition of the binding of the radiolabeled fragment to S-specific antibodies by the synthetic peptide betaS(1-13). These antibodies, which appear monospecific, can be used to study the conformation of the NH2-terminal region of the beta chain of HbS.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D005779	Immunodiffusion	Technique involving the diffusion of antigen or antibody through a semisolid medium, usually agar or agarose gel, with the result being a precipitin reaction.	Gel Diffusion Tests,Diffusion Test, Gel,Diffusion Tests, Gel,Gel Diffusion Test,Immunodiffusions,Test, Gel Diffusion,Tests, Gel Diffusion
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
D006451	Hemoglobin, Sickle	An abnormal hemoglobin resulting from the substitution of valine for glutamic acid at position 6 of the beta chain of the globin moiety. The heterozygous state results in sickle cell trait, the homozygous in sickle cell anemia.	Hemoglobin S,Deoxygenated Sickle Hemoglobin,Deoxyhemoglobin S,Hemoglobin SS,Hemoglobin, Deoxygenated Sickle,SS, Hemoglobin,Sickle Hemoglobin,Sickle Hemoglobin, Deoxygenated
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
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
D000906	Antibodies	Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining