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  • 1
    Electronic Resource
    Electronic Resource
    Synthesis, biological activity and autoimmune recognition of the hormone-binding regions of the human thyrotropin receptor (1992)
    Springer
    The protein journal 11 (1992), S. 417-419 
    Details
    ISSN: 1573-4943
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01673778
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Production of anti-human thyroglobulin and anti-thyroid hormone antibodies in rabbits immunized with homogenate of human papillary cancer tissue (1986)
    Springer
    The protein journal 5 (1986), S. 51-57 
    Details
    ISSN: 1573-4943
    Keywords: anti-human thyroglobulin antibodies ; anti-thyroid hormone antibodies ; papillary cancer ; thyroglobulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Papillary cancer tissue of the thyroid gland removed from each of three patients was homogenized in phosphate buffer followed by centrifugation. Each of three rabbits was immunized with each of the supernatants (TC-1, TC-2, TC-3). These rabbits were immunized on days 0, 7, 14, and 21, and serum from each rabbit, obtained 4 weeks after the first immunization, was examined for the presence of anti-human thyroglobulin (HTg), anti-thyroxine (T4), and anti-triiodothyronine (T3) antibodies. Production of anti-HTg antibodies was observed in all three rabbits. In addition, despite the low content of iodine, T3, and T4 in thyroglobulin that had been purified from the papillary cancer tissues (p-HTg), production of anti-T4 and anti-T3 was observed in two of the three rabbits, and the other immunized with TC-1 showed anti-T4 but no anti-T3 antibodies. The significance of the production of anti-thyroid hormone antibodies in rabbits with respect to the antigenic structure of p-HTg with low content of iodine and thyroid hormone is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025583
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Thyroxine binding to human serum albumin immobilized on sepharose and effects of nonprotein albumin-binding plasma constituents (1990)
    Springer
    The protein journal 9 (1990), S. 461-465 
    Details
    ISSN: 1573-4943
    Keywords: Thyroxine ; albumin ; fatty acid ; bilirubin ; ANS ; steroid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract 125I-thyroxine (125I-T4) binding to human serum albumin (HSA) covalently attached onto CNBr-activated Sepharose (HSA-Sepharose) was studied.125I-T4 binding to HSA-Sepharose was rapid and saturable. Nonlinear curve-fitting analysis of binding isotherms revealed two classes of binding sites. The values of dissociation constants of high and low affinity sites were 2.19±0.53×10−6 M and 2.69±0.78×10−5 M, respectively. The number of binding sites of the high and the low affinity sites were 1.28±0.46 mol/mol and 23.5±9.7 mol/mol of HSA, respectively. Fatty acids and bilirubin competitively inhibited the high-affinity binding of125I-T4 to HSA-Sepharose without affecting the low-affinity binding. 8-anilino-1-naphthalene sulfonic acid (ANS) inhibited the high affinity T4 binding via reduction of the binding capacity. Unlabeled T4 showed little inhibition of ANS binding to HSA, as measured by fluorescence intensity. These results suggest that ANS allosterically inhibits the high-affinity T4 binding to HSA-Sepharose.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024622
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  • 4
    Electronic Resource
    Electronic Resource
    Autoimmune recognition of thyroglobulin and thyroid hormones in rabbits (1986)
    Springer
    The protein journal 5 (1986), S. 407-415 
    Details
    ISSN: 1573-4943
    Keywords: Rabbit thyroglobulin ; anti-thyroid hormone antibodies ; anti-thyroglobulin antibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Two rabbits (RG-1, RG-2) were immunized with rabbit thyroglobulin (RTg) purified from thyroid glands of four other normal rabbits of the same strain, and bled serially. Antisera were obtained at different times after the first immunization and kept separately and studied. Production of anti-RTg as well as anti-thyroid hormone antibodies such as anti-thyroxine (T4) and anti-triiodothyronine (T3) antibodies was observed in both rabbits. Physicochemical parameters of anti-RTg antibodies with RTg, T4, and T3 were calculated in two selected antisera (70-day and 253-day) of each of the rabbits, using a Scatchard plot. Extraction of serial sera from both rabbits disclosed the presence of larger amounts of T3 and T4 in immune sera than in preimmune serum. Examination of pathology of thyroid glands and kidneys in both rabbits was negative for the lesions of autoimmune thyroiditis and immune nephritis. These results indicate that anti-Tg as well as anti-thyroid hormone autoantibodies can be raised without thyroid pathology in rabbit by immunization with autologous Tg.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025573
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  • 5
    Electronic Resource
    Electronic Resource
    Localization and synthesis of an insulin-binding region on human insulin receptor (1990)
    Springer
    The protein journal 9 (1990), S. 229-233 
    Details
    ISSN: 1573-4943
    Keywords: Insulin ; insulin receptor ; binding site ; synthetic peptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Seven regions of the α subunit of human insulin receptor (HIR) were synthesized and examined for their ability to bind radioiodinated insulin. A peptide representing one of these regions (namely, residues α655–670) exhibited a specific binding activity for insulin. In quantitative radiometric titrations, the binding curves of125I-labeled insulin to adsorbents of peptide α655–670 and of purified placental membrane were similar or superimposable. The binding of radioiodinated insulin to peptide or to membrane adsorbents was completely inhibited by unlabeled insulin, and the inhibition curves indicated that the peptide and the membrane on the adsorbents had similar affinities. Synthetic peptides that were shorter (peptide α661–670) or longer (peptide α651–670) than the region α655–670 exhibited lower insulin-binding activity. It was concluded that an insulin-binding region in the HIR α subunit resides within residues α655–670. The results do not rule out the possibility that other regions of the α subunit may also participate in binding of HIR to insulin, with the region described here forming a “face” within a larger binding site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025313
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  • 6
    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
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