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  • 1
    Electronic Resource
    Electronic Resource
    Amino acid substitutions outside a preselected antigenic region in hemoglobin affect the binding to monoclonal antibodies obtained by immunization with the synthetic region (1993)
    Springer
    The protein journal 12 (1993), S. 403-412 
    Details
    ISSN: 1573-4943
    Keywords: Monoclonal antibody ; synthetic peptide ; hemoglobin ; amino acid substitution ; antigenic site
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract It is often assumed that amino acid substitutions outside a protein antigenic site have no effect on the reactivity of a protein variant with antibodies, especially monoclonal antibodies (mAbs). Substitutions that exert an effect on the reactivity of a protein variant with mAbs are frequently considered to be within the antigenic site of the mAb. To test this assumption, two mAbs [IgGl(k) and IgG2a (k)] were prepared by immunization with a synthetic peptide corresponding to region 63–78 of the α chain of human hemoglobin (Hb). The peptide was used as an immunogen in its free form (i.e., without conjugation to a carrier), so that the results will not be made ambiguous by peptide modification nor by an immune response to sites spanning peptide and protein carrier. In addition to their reaction with human Hb, the mAbs were also studied with four primate Hbs which had no substitutions within region α63–78 and only a limited number of substitutions which occurred outside of, and at considerable distances in three-dimensional (3D) structure from, this region. Inhibition studies revealed substantial differences in the binding affinities of some of the primate Hbs, relative to human Hb. Some of the substitutions caused major decreases in binding, although they were at considerable distances in the 3D structure from the indicated site residues. It is concluded that substitutions in a protein, even when distant from an antigenic site, can exert major influences on the protein's reactivity with anti-site mAbs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025040
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  • 2
    Electronic Resource
    Electronic Resource
    Binding of thyroid hormones to human hemoglobin and localization of the binding site (1990)
    Springer
    The protein journal 9 (1990), S. 743-750 
    Details
    ISSN: 1573-4943
    Keywords: Human red cell ; cytosol ; hemoglobin ; thyroid hormone receptor ; nonhemoglobin protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Radiolabeled thyroid hormones were allowed to bind to erythrocyte cytosol and the complex was fractionated by Sephadex G-100 or by high-performance liquid chromatography (HPLC). On Sephadex G-100, four radioactive peaks (P1∼P4) were obtained, whereas HPLC gave only three radioactive peaks (P1∼P3). Chromatographic studies with human adult Hb and non-Hb cytosol protein fractions, which had been reacted with radiolabeled thyroid hormones, and immune precipitation with specific antisera for the hormones, confirmed that the first peak of Sephadex G-100 radioactivity was a mixture of Hb and non-Hb proteins, while the second peak was Hb. The third peak was free125I and the fourth peak was unbound125I-T3 or125I-T4. The third peak of HPLC was confirmed to be a mixture of free125I and unbound radiolabeled thyroid hormones. Scatchard analysis of the interaction between T4 and apo-Hb, and the α- and β-chains of human Hb suggested the presence of the specific binding site(s) for the hormone. Interaction between T4 and synthesized peptides, which constitute the heme pocket of the β-chain of Hb (β61–75, β71–85, β81–95), indicated that the T4 binding site of Hb resides within the heme-binding cavity. It is concluded that human erythrocyte cytosol does not contain “receptor” for thyroid hormones and cannot be a model for studying functions of cytosol “receptor” for the hormones; rather, it contains binding protein with large binding capacity, including Hb and non-Hb proteins, which possibly constitute a large reservoir for the hormone in blood.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024769
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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