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Radiohalogenation of Antibodies: Chemical Aspects

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Radiolabeled Monoclonal Antibodies for Imaging and Therapy

Part of the book series: NATO ASI Series ((NSSA,volume 152))

Abstract

Proteins have been labeled with halogen isotopes for many years. These tracers have been exploited as probes of protein metabolism and pharmacokinetics in vivo and have provided invaluable tools for use in radioimmunoassay. Because of this extensive experience with radioiodinated proteins and the direct applicability of in vitro data obtained with I-125, labeling with halogen isotopes has been an attractive approach to the development of monoclonal antibodies as agents for radioimmunodiagnostic and therapeutic applications.

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References

  1. V. I. Vedeneyev, L. V. Gurvich, V. N. Kondrat’yev, V. A. Medvedev and Y. L. Frankevich, “Bond Energies, Ionization Potentials and Electron Affinities”, St. Martin’s Press, New York (1966).

    Google Scholar 

  2. K. Berei and L. Vasaros, Organic chemistry of astatine, Hungarian Academy of Sciences Report KFKI-1981-10 p, 41 (1981).

    Google Scholar 

  3. A. S. McFarlane, Efficient trace-labelling of proteins with iodine, Nature 182:53 (1958).

    Article  PubMed  CAS  Google Scholar 

  4. U. Rosa, G. A. Scassellati, F. Pennisi, N. Riccioni, P. Giagnoni, and R. Giordani, Labelling of human fibrinogen with I-131 by electrolytic iodination, Biochem. Biophys. Acta 86:519 (1964).

    Article  PubMed  CAS  Google Scholar 

  5. W. M. Hunter and F. C. Greenwood, Preparation of iodine-131 labelled human growth hormone of high specific activity, Nature 194:495 (1962).

    Article  PubMed  CAS  Google Scholar 

  6. M. A. K. Markwell, A new solid state reagent to iodinate proteins, Anal. Biochem. 125:427 (1983).

    Article  Google Scholar 

  7. W. R. Butt, The iodination of Follicle-stimulating and other hormones for radioimmunoassay, Enocrinology 55:453 (1972).

    Article  CAS  Google Scholar 

  8. F. Tejedor and J. P. G. Ballesta, Iodination of biological samples without loss of functional activity, Anal. Biochem. 127:143 (1982).

    Article  PubMed  CAS  Google Scholar 

  9. J. J. Marchalonis, An enzymatic method for the trace iodination of immunoglobulins and other proteins, Biochem. J. 113:299 (1969).

    PubMed  CAS  Google Scholar 

  10. L. Knight, K. A. Krohn, M. J. Welch, B. Spomer and L. P. Hager, Br-77: A new protein label, in: “Radiopharmaceuticals”, G. Subramanian, B. A. Rhodes, J. F. Cooper, and V. J. Sodd, eds., Society of Nuclear Medicine, New York (1975).

    Google Scholar 

  11. K. D. McElvany and M. J. Welch, Characterization of bromine-77-labeled proteins prepared using bromoperoxidase, J. Nucl. Med. 21:953 (1980).

    PubMed  CAS  Google Scholar 

  12. G. S. David, Solid state lactoperoxidase:. A highly stable enzyme for simple, gentle iodination of proteins, Biochem. Biophys. Res. Comm. 48:464 (1972).

    Article  PubMed  CAS  Google Scholar 

  13. G. S. David and R. A. Reisfeld, Protein iodination with solid state lactoperoxidase, Biochem. 13:1014 (1974).

    Article  CAS  Google Scholar 

  14. P. J. Fraker and J. C. Speck, Protein and cell membrane iodinations with a sparingly soluble chloramide 1,3,4,6-tetrachloro-3 α-6α-diphenylglycouril, Biochem. Biophys. Res. Comm. 80:849 (1978).

    Article  PubMed  CAS  Google Scholar 

  15. M. R. Zalutsky, D. F. Hayes, and D. W. Kufe, Radioiodination of DF3 antibody: Optimization using in vitro binding assays, J. Label. Cmpd. Radiopharm. (in press).

    Google Scholar 

  16. P. Reay, Use of N-bromosuccinimide for the iodination of proteins for radioimmunoassay, Ann. Clin. Chem. 19:129 (1982).

    CAS  Google Scholar 

  17. A. E. Bolton and W. M. Hunter, The labelling of proteins to high specific activities by conjugation to a I-125-containing acylating agent, Biochem. J. 133:529 (1973).

    PubMed  CAS  Google Scholar 

  18. A. E. Bolton, V. Lee-Own, R. Kramer McLean, and G. S. Challand, Three different radioiodinat ion methods for human spleen ferritin compared, Clin. Chem. 25:1826 (1979).

    PubMed  CAS  Google Scholar 

  19. V. S. Chang, H. W. Cho, and H. Y. Meltzer, Labeling of creatinine phosphokinase without loss of enzyme activity, Biochem. Biophys. Res. Comm. 65:413 (1975).

    Article  Google Scholar 

  20. L. C. Knight, S. S. L. Harwig and M. J. Welch, In vitro stability and in vivo clearance of fibrinogen or serum albumin labeled with Br-77, I-131, I-125 by direct or indirect synthetic methods, J. Nucl. Med. 18:282 (1977).

    PubMed  CAS  Google Scholar 

  21. F. T. Wood M. M. Wu, and J. C. Gerhart, The radioactive labeling of proteins with an iodinated amidation reagent, Anal. Biochem. 69:339 (1975).

    Article  PubMed  CAS  Google Scholar 

  22. C. E. Hayes and I. J. Goldstein, Radioiodinat ion of sulfhydryl-sensitive proteins, Anal. Biochem. 67:580 (1975).

    Article  PubMed  CAS  Google Scholar 

  23. M. R. Zalutsky, A. M. Friedman, F. Buckingham, W. Wung, F. P. Stuart, and S. J. Simonian, Synthesis of a non-labile astatine-protein conjugate, J. Label Cmpd Radiopharm. 13:181 (1977).

    CAS  Google Scholar 

  24. G. W. Barendsen, T. L. J. Beusker, A. J. vergroesen, and L. Budke, Effects of different ionizing radiations on human cells in tissue culture, Radiation Res. 13:841 (1960).

    Article  PubMed  CAS  Google Scholar 

  25. E. L. Lloyd, M. A. Gammell, C. B. Henning, D. S. Ganmell, and B. J. Zabransky, Cell survival following multiple-track alpha particle irradiation Int. J. Radiat. Biol. 35:23 (1979).

    Article  CAS  Google Scholar 

  26. C. Aaij, W. R. J. M. Tschrotts, L. Lendner, and T. E.W. Feltkamp, The preparation of astatine labeled proteins, Int. J. Appl. Radiat. Isot. 26:25 (1975).

    Article  PubMed  CAS  Google Scholar 

  27. A. T. M. Vaughan and J. H. Fremlin, The preparation of astatine labeled proteins using an electrophilic reaction, Int. J. Nucl., Med. Biol. 5:229 (1978).

    Article  CAS  Google Scholar 

  28. G. W. M. Visser, E. L. Diemer, and F. M. Kaspersen, The preparation and stability of astatotyrosine and astatoiodotyrosine, Int. J. Appl. Radiat. Isot. 30:749 (1979).

    Article  CAS  Google Scholar 

  29. G. W. M. Visser, E. L. Diemer, and F. M. Kaspersen, The nature of the astatine-protein bond, Int. J. Appl. Radiat. Isot. 32:905 (1981).

    Article  CAS  Google Scholar 

  30. A. M. Friedman, M. R. Zalutsky, W. Wung, F. Buckingham, P. V. Harper, G. H. Sherr, B. Wainer, R. L. Hunter, E. H. Appelman, R. M. Rothberg, F. W. Fitch, F. P. Stuart, and S. J. Simonian, Preparation of a biologically stable and immunogenically competent astatinated protein, Int. J. Nucl. Med. Biol. 4:219 (1977).

    Article  PubMed  CAS  Google Scholar 

  31. A. T. M. Vaughan, The labeling of proteins with At-211 using an acylation reaction, Int. J. Appl. Radiat. Isot. 30:576 (1979).

    Article  CAS  Google Scholar 

  32. A. Harrision and L. Royle, Preparation of a At-211-IgG conjugate which is stable in vivo, Int. J. Appl. Radiat. Isot. 35:1005 (1984).

    Article  Google Scholar 

  33. A. T. M. Vaughan, W. J. Bateman, and J. Cowan, The preparation and cytotoxic properties of 211At labelled concanavalin A bound to cell membranes, J. Radioanal. Chem. 64:33 (1981).

    Article  CAS  Google Scholar 

  34. A. T. M. Vaughan, W. J. Bateman, And D. R. Fisher, The in vivo fate of a 211At labelled monoclonal antibody with known specificity in a murine system, Int. J. Radiat. Oncol. Biol. Phys. 8:1943 (1982).

    Article  PubMed  CAS  Google Scholar 

  35. A. T. M. Vaughan, W. J. Bateman, G. Brown, and J. Cowan, The specific inhibition of cellular clonogenic proliferation using At-211 labelled lectins and antibodies-I, Int. J. Nucl. Med. Biol. 9:167 (1982).

    Article  PubMed  CAS  Google Scholar 

  36. W. J. Bateman, A. T. M. Vaughan, and G. Brown, Tumour localization of 211At labelled monoclonal antibody to a subcutaneous human heterograft in the nude mouse II, Int. J. Nucl. Med. Biol. 4:241 (1983).

    Article  Google Scholar 

  37. E. A. Kabat, T. T. Wu, and H. Bilofsky, Immunoglobulin sequences, NIH Publication No. 80-2008, p1, NIH, Bethesda, MD. (1979).

    Google Scholar 

  38. B. -K. Seon, O. A. Robolt and D. Pressman, Reactivity of tyrosine residues in the constant portion of type K Bence Jones protein, Biochem. Biophys. Acta. 200:81 (1970).

    Article  PubMed  CAS  Google Scholar 

  39. S. K. Dube, O. A. Roholt and D. Pressman, Relative reactivity to iodination of tyrosine residues in α-chymotrypsin, J. Biol. Chem. 241:4665 (1965).

    Google Scholar 

  40. A. L. Grossberg, G. Radzimski, and D. Pressman, Effect of iodination on the active site of several antihapten antibodies, Biochem. 1:391 (1962).

    Article  CAS  Google Scholar 

  41. Y. Shechter, Y. Burstein, and A. Patchornik, Selective oxidation of methionine residues in proteins, Biochem. 14:4497 (1975).

    Article  CAS  Google Scholar 

  42. N. M. Alexander, Oxidative cleavage of tryptophanyl peptide bonds during chemical-and peroxidase-cata1yzed iodinations, J. Biol. Chem. 249:1946 (1974).

    PubMed  CAS  Google Scholar 

  43. L. A. Sherman, S. Harwig, and O. A. Hayne, Macromolecular complexes formed as the result of chloramine-T radio-iodination of proteins, Int. J. Appl. Radiat. Isot. 25:81 (1974).

    Article  PubMed  CAS  Google Scholar 

  44. D. F. Hayes, M. R. Zalutsky, W. Kaplan, M. Noska, A. Thor, D. Colcher, and D. W. Kufe, Pharmacokinetics of radiolabeled monoclonal antibody B6.2 in patients with metastatic breast cancer, Cancer Res. 46:3157 (1986).

    PubMed  CAS  Google Scholar 

  45. D. C. Sullivan, J. S. Silva, C. E. Cox, D. E. Haagensen, Jr., C. C. Harris, W. H. Briner, and S. A. Wells, Jr., Localization of I-131 labeled goat and primate anti-carcinoembryonic antigen (CEA) antibodies in patients with cancer, Invest. Radiol. 17:350 (1982).

    Article  PubMed  CAS  Google Scholar 

  46. P. Dumas, Deshalogenation de divers derives iodes phenoliques chez le rat normal et. thyroidectomise, Biochem. Pharmacol. 22:1599 (1973).

    Article  PubMed  CAS  Google Scholar 

  47. W. Tong, A. Taurog, and I. L. Chaikoff, The metabolism of I-131-labeled diiodotyrosine, J. Biol. Chem. 207:59 (1954).

    PubMed  CAS  Google Scholar 

  48. J. B. Stanbury and M. L. Morris, Deiodination of diodotyrosine by cell-free systems, J. Biol. Chem. 233:106 (1958).

    PubMed  CAS  Google Scholar 

  49. I. J. Chopra, A study of extrathyroidal conversion of thyroxine (T4) to 3, 3′, 5,-triiodothyronine (T3) in vitro, Endocrinology 101:453 (1977).

    Article  PubMed  CAS  Google Scholar 

  50. M. M. Kaplan and R. D. Utiger, Iodothyronine metabolism in rat liver homogenates J. Clin. Invest. 61:459 (1978).

    Article  PubMed  CAS  Google Scholar 

  51. R. Ientile, S. Macaione, P. Russo, G. Pugliese, and R. DiGiorgio, Phenolic and tyrosyl ring deiodination in thyroxine from rat retina during postnatal development, Eur. J. Biochem. 142:15 (1984).

    Article  PubMed  CAS  Google Scholar 

  52. R. C. Smallridge and N. E. Whorton, 3′-monoiodothyronine degradation in rat liver homogenate: Enzymatic characteristics and documentation of deiodination by high-pressure liquid chromatography Metabolism 33:1034 (1984).

    Article  PubMed  CAS  Google Scholar 

  53. R. C. Smallridge, K. D. Burman, K. E. Ward, L. Wartofsky, R. C. Dimond, F. D. Wright, and K. R. Latham, 3′,5′ -diiodothyronine to 3′-mono-iodothyronine conversion in the fed and fasted rat: Enzyme characteristics and evidence for two distinct S′-deiodinases, Endocrinology 108:2336 (1981).

    Article  PubMed  CAS  Google Scholar 

  54. J. L. Leonard and I. N. Rosenbert, Subcellular distribution of thyroxine S′-deiodinase in the rat kidney: A plasma membrane location, Endocrinology 103:274 (1977).

    Article  Google Scholar 

  55. M. R. Zalutsky, D. Colcher, W. Kaplan, And D. F. Kufe, Radioiodinated B6.2 monoclonal antibody: Further characterization of a potential radiopharmaceutical for the identification of breast tumors, Int. J. Nucl. Med. Biol. 12:227 (1985).

    Article  PubMed  CAS  Google Scholar 

  56. D. S. Wilbur, D. S. Jones, A. R. Fritzberg, and A. C. Morgan, Radioiodination of monoclonal antibodies, Labeling with para-iodophenyl (PIP) derivatives for in vivo stability of the radioiodine label, J. Nucl. Med. 27:959 (1986) abstract.

    Google Scholar 

  57. J. L. Goldstein and M. S. Brown, Binding and degradation of low density lipoproteins by cultured human fibroblasts, J. Biol. Chem. 249:5153 (1974).

    PubMed  CAS  Google Scholar 

  58. S. Terris and D. F. Steiner, Binding and degradation of I-125-insulin by rat hepatocytes, J. Biol. Chem. 250:8389 (1975).

    PubMed  CAS  Google Scholar 

  59. G. Carpenter and S. Cohen, 125I-labeled human epidermal growth factor: Binding, internalization and degradation in human fibroblasts, J. Cell Biol. 71:159 (1976).

    Article  PubMed  CAS  Google Scholar 

  60. A. S. H. DeJong, J. M. W. Bouma, and M. Gruber, O-(4-diazo-3,5-di[I-125]iodobenzoy1-sucrose, a novel radioactive label for determining organ sites of catabolism of plasma proteins, Bio. Chem. J. 198:45 (1981).

    CAS  Google Scholar 

  61. R. C. Pittman, T. E. Carew, C. K. Glass, S. R. Green, C. A. Taylor, Jr., and A. D. Attie, A radioiodinated, intracellularly trapped ligand for determining the sites of plasma protein degradation in vivo, Biochem. J. 212:791 (1983).

    PubMed  CAS  Google Scholar 

  62. M. R. Zalutsky and A. Narula, A method for the radiohalogenation of proteins resulting in decreased thyroid uptake of radioiodine, Appl. Radiat. Isot. 38:1051 (1987).

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Department of Radiology, Duke University Medical Center, Durham, NC, USA

    Michael R. Zalutsky

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  1. Michael R. Zalutsky
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  1. Brookhaven National Laboratory, Upton, New York, USA

    Suresh C. Srivastava

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Zalutsky, M.R. (1988). Radiohalogenation of Antibodies: Chemical Aspects. In: Srivastava, S.C. (eds) Radiolabeled Monoclonal Antibodies for Imaging and Therapy. NATO ASI Series, vol 152. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5538-0_15

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  • DOI: https://doi.org/10.1007/978-1-4684-5538-0_15

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