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Zusammenfassung

During the last few years isotopes have become one of the most important tools of the biochemists. Isotopically labeled molecules behave, in general, in the same manner as their unlabeled analogues. They allow us, however, to differentiate molecules formed after administration of the isotope from those formed before, and thus enable us to obtain more insight into the site and rate of formation of metabolites. Therefore, we may obtain information on the precursors of metabolites, their turn-over time and their breakdown products. For the same reason, isotopically labeled antigens have been used in immunochemical research. Tracing of isotopically labeled antigens has provided new information on their elimination from the circulation, their deposition in certain tissues or cells, their metabolic fate and their breakdown. In vitro experiments with labeled antigens allow us to measure their incorporation into antigen-antibody complexes. In animals injected with isotopically labeled amino acids, incorporation of these amino acids into antibody molecules can be measured. This enables us to determine the rate of antibody formation. Finally, experiments with isotopically labeled complement give some information on the components of the complement complex which combine with antigen-antibody aggregates. It is clear from this short survey that the application of isotopes enables us to investigate numerous problems which were inaccessible to experimental research prior to the availability of isotopes.

The experimental work described in this article has been supported by research grants from the National Science Foundation (G 5468) and the U.S. Public Health Service (C-1852), and by contracts of Indiana University with the Office of Naval Research (NR 108–035) and the Atomic Energy Commission [AT(11–1)209]. I am particularly grateful to Dr. Audrie N. Roberts for critical reading of the manuscript and for many helpful suggestions.

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References

  • Almond, A. E., G. E. Francis, J. D. Hawkins and A. Wormall: The fate of intravenously injected antigenic proteins and haptens in immune and normal rabbits. Proc. 2nd Radioisotope Conf. Oxford 1954, p. 360.

    Google Scholar 

  • Askonas, B. A. : Protein synthesis in mammalian cells with particular reference to antibody formation. Rec. Trav. chim. Pays-Bas 77, 611 (1958).

    CAS  Google Scholar 

  • Askonas, B. A., and J. H. Humphrey: Formation of specific antibodies and γ-globulin in vitro. Astudy of the synthetic ability of various tissues from rabbits immunized by different methods. Biochem. J. 68, 252 (1958a).

    PubMed  CAS  Google Scholar 

  • Askonas, B. A., and J. H. Humphrey: Formation of antibody by isolated perfused lungs of immunized rabbits. The use of [14C] amino acids to study the dynamics of antibody secretion. Biochem. J. 70, 212 (1958b).

    PubMed  CAS  Google Scholar 

  • Askonas, B. A., and J. H. Humphrey: and R. R. Porter: On the origin of the multiple form of rabbit γ-globulin. Biochem. J. 63, 412 (1956).

    PubMed  CAS  Google Scholar 

  • Askonas, B. A., J. L. Simkin and T. S. Work: Nucleic acids and protein synthesis in animal tissues. Biochem. Soc. Sympos. No 14, 32 (1957).

    Google Scholar 

  • Askonas, B. A., and R. G. White : Sites of antibody production in the guinea pig. The relation between in vitrosynthesis of anti-ovalbumin and γ-globulin and distribution of antibody containing plasma cells. Brit. J. exp. Path. 37, 61 (1956).

    PubMed  CAS  Google Scholar 

  • Banks, T. E., G.E. Francis, W. Mulligan and A. Wormall: The precipitin reaction and antibody valence studied with the aid of radioactive isotopes. Nature (Lond.) 165, 111 (1950).

    PubMed  CAS  Google Scholar 

  • Banks, T. E., G.E. Francis, W. Mulligan and A. Wormall :The use of radioactive isotopes in immunological investigations. 6. Some observations on precipitin inhibition tests and on antibody valence. Biochem J. 48, 371 (1951).

    PubMed  CAS  Google Scholar 

  • Berenbaum, M. C. : Autoradiographic localization and measurement of intracellular antibody, using labelled antigen. Nature (Lond.) 177, 46 (1956).

    CAS  Google Scholar 

  • Berenbaum, M. C. : The antibody content of single cells. J. clin. Path. 11, 543 (1958).

    PubMed  CAS  Google Scholar 

  • Berenbaum, M. C. : The autoradiographic localization of intracellular antibody. Immunology 2, 71 (1959).

    PubMed  CAS  Google Scholar 

  • Berson, S. A., and R. S. Yalow: Ethanol fractionation of plasma and electrophoretic identification of insulin-binding activity. J. clin. Invest. 36, 642 (1957).

    PubMed  CAS  Google Scholar 

  • Biozzi, G., N. Benacerraf, C. Stiffel, B. N. Halpern and D. Mouton: Influence of the amount of iodine fixed on serum proteins, normal or heat-modified, on the phagocytosis of these colloids by the cells of the reticuloendothelial system. Ann. Inst. Pasteur 92, 89 (1957).

    CAS  Google Scholar 

  • Blau, M., A. C. Johnson and D. Pressman: p-Iodobenzoyl groups as paired label for in vivoprotein distribution studies : specific localization of anti-tissue antibodies. Int. J. appl. Radiat. 3, 217 (1958).

    PubMed  CAS  Google Scholar 

  • Burnet, F. M. : A modification of Jerne’s theory of antibody production using the concept of clonal selection. Aust. J. Sci. 20, 67 (1957).

    Google Scholar 

  • Butement, F. D. S. : Introduction of radioactive tracers into antisera. Nature (Lond.) 162, 731 (1948).

    CAS  Google Scholar 

  • Calvin, M. : Isotopic carbon, techniques in its measurement and chemical manipulation. 376 pp. New York: J. Wiley 1949.

    Google Scholar 

  • Campbell, D.H.: Some speculations on the significance of formation and peristence of antigen fragments in tissues of immunized animals. Blood 12, 589 (1957).

    PubMed  CAS  Google Scholar 

  • Catch, J. R. : Carbon-14 amino acids from chlorella. Radioisotope Conf. 1, 258 (1954). New York: J. E. J.hnston, Pub., Academic Press, Inc.

    Google Scholar 

  • Cheng, H. F., and F. Haurowitz: Incorporation of 35S-amino acids into antibodies in primary and secondary response. Fed. Proc. 16, 409 (1957).

    Google Scholar 

  • Cheng, H. F., and F. Haurowitz: Details of this work are described in the Ph. D. thesis of H. F. Cheng (Indiana University 1957). 128 pp.

    Google Scholar 

  • Clayton, R. M., and M. Feldman: Detection of antigens in the embryo by labelled antisera. Experientia (Basel) 11, 29 (1955).

    PubMed  CAS  Google Scholar 

  • Cohen, S.: Determination of antibody through the use of I131label: experiments with equine diphtheria antitoxin. J. Immunol. 67, 339 (1951).

    PubMed  CAS  Google Scholar 

  • Cohen, S.: R. C. Holloway, C. Matthews and A. S. McFarlane: Distribution and elimination of 131I- and 14C-labelled plasma proteins in the rabbit. Biochem J. 62, 143 (1956).

    PubMed  CAS  Google Scholar 

  • Crampton, C. F., and F. Haurowitz: Deposition of small doses of injected antigen in rabbits. J. Immunol. 69, 457 (1952).

    PubMed  CAS  Google Scholar 

  • Crampton, C. F., H. H. Reller and F. Haurowitz: Persistence of C14-anthranil-azoovalbumin in injected rabbits. Proc. Soc. exp. Biol. (N. Y.) 80, 448 (1952).

    CAS  Google Scholar 

  • Crampton, C. F., H. H. Reller and F. Haurowitz: Deposition of beef serum gammaglobulin in rabbit organs and subcellular fractions. J. Immunol. 71, 319 (1953).

    PubMed  CAS  Google Scholar 

  • Crampton, C. F., J. L. Rodeheaver and F. R. Frankel: The fate of iodoproteins in specifically unresponsive rabbits. Fed. Proc. 18, 208 (1959).

    Google Scholar 

  • Crawhall, J. C., J. D. Hawkins and D. G. Smyth: The biosynthesis of a tritium-labelled antibody. Biochem J. 69, 286 (1958).

    PubMed  CAS  Google Scholar 

  • Dixon, F. J., and P.H. Maurer: Fate of antibody following in vivocombination with specific antigen. Proc. Soc. exp. Biol. (N.Y.) 84, 442 (1953).

    CAS  Google Scholar 

  • Dixon, F. J., and P.H. Maurer: and M. P. Deichmiller: Primary and specific anamnestic antibody responses of rabbits to heterologous serum protein antigens. J. Immunol. 72, 179 (1954).

    PubMed  CAS  Google Scholar 

  • Dixon, F. J., and D. W. Talmage : Catabolism of I131labelled bovine gamma globulin in immune and non-immune rabbits. Proc. Soc. Exp. Biol. (N.Y.) 78, 123 (1951).

    CAS  Google Scholar 

  • Dixon, F. J., and D. W. Talmage : P.H. Maurer and M. Deichmiller: The half-life of homologous gamma globulin (antibody) in several species. J. exp. Med. 96, 313 (1952).

    CAS  Google Scholar 

  • Eisen, H. N., and A. S. Keston: Measurement and study of immune precipitates by means of ultraviolet absorption spectroscopy. Fed. Proc. 7, 153 (1948).

    Google Scholar 

  • Eisen, H. N., and A. S. Keston: The immunologic reactivity of bovine serum albumin labelled with trace-amounts of radioactive iodine (I131). J. Immunol. 63, 71 (1949).

    PubMed  CAS  Google Scholar 

  • Eisen, H. N., H. S. Penefsky and M. Tabachnick: Detection of antigen-antibody interaction by means of electrophoresis in paper. Fed. Proc. 14, 461 (1955).

    Google Scholar 

  • Farr, R. S. : A quantitative immunochemical measure of the primary interaction between P-BSA and antibody. J. infect. Dis. 103, 239 (1958).

    PubMed  CAS  Google Scholar 

  • Fields, M., and R. L. Libby: Uptake of labeled antigens by the mitochondria of mouse liver. J. Immunol. 69, 581 (1952).

    PubMed  CAS  Google Scholar 

  • Fleischer, S., A. Lietze, H. Walter and F. Htjrowitz: Conversion of serum proteins into tissue proteins. Proc. Soc. exp. Biol. (N.Y.) 101, 860 (1959).

    PubMed  CAS  Google Scholar 

  • Francis, G. E., and J.D. Hawkins: The use of radioactive isotopes in immunological investigations. 11. The fate of some chemically modified protein antigens in normal and immune rabbits. Biochem. J. 65, 570 (1957).

    PubMed  CAS  Google Scholar 

  • Francis, G. E., and J.D. Hawkins:The use of radioactive isotopes in immunological investigations. 13. The role of leucocytes and non-plasma antibody in the removal of antigenic proteins from the blood stream of immunized rabbits. Biochem. J. 69, 287 (1958).

    PubMed  CAS  Google Scholar 

  • Francis, G. E., and J.D. Hawkins: and A. Wormall: The use of radioactive isotopes in immunological investigations. 10. The fate of some intravenously injected native proteins in normal and immune rabbits. Biochem. J. 65, 560 (1957).

    PubMed  CAS  Google Scholar 

  • Francis, G. E., W. Mulligan and A. Wormall: Labelling of proteins with iodine-131, sulphur-35 and phosphorus-32. Nature (Lond.) 167, 748 (1951).

    CAS  Google Scholar 

  • Francis, G. E., W. Mulligan and A. Wormall: The use of radioactive isotopes in immunological investigations. 7. Labelled proteins and protein antigens containing both iodine and mustard gas sulphone groups. Biochem. J. 60, 118 (1955a).

    PubMed  CAS  Google Scholar 

  • Francis, G. E., W. Mulligan and A. Wormall: The use of radioactive isotopes in immunological investigations. 8. Labelling antibodies with 131I and 35S. Biochem. J. 60, 363 (1955b).

    PubMed  CAS  Google Scholar 

  • Francis, G. E., W. Mulligan and A. Wormall: The use of radioactive isotopes in immunological investigations. 9. The reactions of antisera to antigens containing multiple determinant groups. Biochem. J. 60, 370 (1955c).

    PubMed  CAS  Google Scholar 

  • Francis, G. E., and A. Wormall: The use of radioactive isotopes in immunological investigations. 1. Precipitin reactions with ovovitellin containing P32. Biochem. J. 42, 469 (1948).

    CAS  Google Scholar 

  • Friedberg, W. : Metabolism of I131-labeled tobacco mosaic virus in spleen and liver. Proc. Soc. exp. Biol. (N.Y.) 99, 541 (1958).

    CAS  Google Scholar 

  • Friedberg, W. : H. Walter and F. Htjrowitz: The fate in rats of internally and externally labelled heterologous proteins. J. Immunol. 75, 315 (1955).

    PubMed  CAS  Google Scholar 

  • Gabrieli, E. R. : The velocity at which radioactive colloids disappear from the blood. Studies on the function of the reticuloendothelial system. Acta physiol. scand. 23, 283 (1951).

    PubMed  CAS  Google Scholar 

  • Garvey, J. S., and D. H. Campbell: Studies of the retention and properties of S35-labelled antigen in livers of immunized rabbits. J. Immunol. 76, 36 (1956).

    PubMed  CAS  Google Scholar 

  • Garvey, J. S., and D. H. Campbell: The retention of S35-labelled bovine serum albumin in normal and immunized rabbit liver tissue. J. exp. Med. 105, 361 (1957).

    PubMed  CAS  Google Scholar 

  • Garvey, J. S., and D. H. Campbell: In vivo identification in liver tissue of an S35-azo label with its protein carrier. Arch. Biochem. 73, 507 (1958).

    PubMed  CAS  Google Scholar 

  • Garvey, J. S., and D. H. Campbell: The in vivo stability of antibody. J. exp. Med. 110, 355 (1959).

    PubMed  CAS  Google Scholar 

  • Gavosto, F., and A. Ficq: Radioactive study of the localization of tobacco mosaic virus antigen. Nature (Lond.) 172, 406 (1953).

    CAS  Google Scholar 

  • Green, H., and H. S. Anker: On the synthesis of antibody protein. Biochem. biophys. Acta 13, 365 (1954).

    CAS  Google Scholar 

  • Grégoire, F., A. S. McFarlane and J. H. Humphrey: Isotopic studies of globulin production in extravascular sites. Radioisotopes in Scientific Research (Proceedings UNESCO International Conference Paris), 1957, p. 247.

    Google Scholar 

  • Gros, P., J. Coursaget and M. Macheboeuf: The existence of protein precursors in the formation of antibodies; studies made with carbon14-labeled valine. Bull. Soc. Chim. biol. (Paris) 34, 1070 (1952).

    CAS  Google Scholar 

  • Gros, P., J. Coursaget J. M. Dubert, S. S. Sung, J. Coursaget and M. Macheboeuf: Use of valine labeled with carbon13in its isopropyl group in the study of the rate of renewal of antibodies and other protein fractions of the blood serum. Bull. Soc. Chim. biol. (Paris) 34, 37 (1952).

    CAS  Google Scholar 

  • Gurvich, A. E., and N. P. Smirnova: The effect of immunization with two antigens on antibody content and rate of glycine-C14inclusion into antibodies. Biokhimya 22, 626 (1957).

    CAS  Google Scholar 

  • Haurowitz, F.: The mechanism of the immunological response. Biol. Rev. 27, 247 (1952).

    Google Scholar 

  • Haurowitz, F.: Mechanisms of Hypersensitivity (J. H. Shaffer, edit.), p. 547. 1958.

    Google Scholar 

  • Haurowitz, F.: The role of the antigen in antibody formation. Immunity and virus infection (V. A. Najjar, edit.), p. 18. 1959.

    Google Scholar 

  • Haurowitz, F., and F. C. Crampton: The role of the nucleus in protein synthesis. Exp. Cell. Res. Suppl. 2, 45 (1952a).

    CAS  Google Scholar 

  • Haurowitz, F., and F. C. Crampton: The fate in rabbits of intravenously injected I131-iodoovalbumin. J. Immunol. 68, 73 (1952b).

    PubMed  CAS  Google Scholar 

  • Haurowitz, F., and F. C. Crampton: and H. H. Keller: Distribution of antigenic and non-antigenic proteins in the organism. Naunyn-Schmiedeberg’s Arch. exp. Path. Pharmak. 219, 11 (1953).

    CAS  Google Scholar 

  • Haurowitz, F., and F. C. Crampton: and R. Sowinski: Immunochemical studies with labelled antigens. Fed. Proc. 10, 560 (1951).

    PubMed  CAS  Google Scholar 

  • Haurowitz, F., S. Fleischer, H. Walter and A. Lietze : The metabolism of isotopically labeled plasma proteins. Proc. Internat. Conference (Geneva) 25, 111 (1959).

    CAS  Google Scholar 

  • Haurowitz, F., W. Friedberg, H. Walter and M. Yenson: The metabolic fate of “internally” and “externally” labelled protein antigens. Proc. Internat. Conference on Peaceful Uses of Atomic Energy, Geneva 12, 545 (1955).

    Google Scholar 

  • Haurowitz, F., H. H. Reller and H. Walter: The metabolic fate of isotopically labelled proteins, azo-proteins and azohaptens. J. Immunol. 75, 417 (1955).

    PubMed  CAS  Google Scholar 

  • Haurowitz, F., R. H. Shellhamer, M. Dicks, E. S. Brown and H. F. Cheng: Localization of antigens by autoradiography. Fed. Proc. 14, 465 (1955).

    Google Scholar 

  • Haurowitz, F., R. Sowinski and H. F. Cheng: The dissociation of antigen-antibody precipitates. J. Amer. chem. Soc. 79, 1882 (1957).

    CAS  Google Scholar 

  • Haurowitz, F., and H. Walter: Stability of an azoprotein hapten in the organism. Proc. Soc. exp. Biol. (N.Y.) 88, 67 (1955).

    CAS  Google Scholar 

  • Hawkins, J. D. : The use of radioactive isotopes in immunological investigations. 12. The binding of a hapten by antibodies in vivo.Biochem. J. 67, 537 (1957).

    PubMed  CAS  Google Scholar 

  • Hawkins, J. D. : Unpublished experiments 1959. —, and F. Haurowitz: Recovery of intravenously injected protein antigens from rat spleens. Biochem. J. 72, P 5 (1959).

    Google Scholar 

  • Humphrey, J. H., and A. S. McFarlane: Fate of homologous antibody in the rabbit. Biochem. J. 57, 195 (1954).

    PubMed  CAS  Google Scholar 

  • Humphrey, J. H., and B. D. Sulitzeanu: The use of [14C] amino acids to study sites and rates of antibody synthesis in living hyperimmune rabbits. Biochem. J. 68, 146 (1958).

    PubMed  CAS  Google Scholar 

  • Ingraham, J. S. : Artificial radioactive antigens. I. Preparation and evaluation of S35- sulfanilic acid-azo-bovine-γ-globulin. II. The metabolism of S35-sulfanilic acid-azo- bovine-γ-globulin in normal and immune mice. J. infect. Dis. 89, 109 (1951).

    PubMed  CAS  Google Scholar 

  • Ingraham, J. S. Artificial radioactive antigens. III. S35-sulfanil-azosheep red cell stromata; preparation and gross distribution in normal rabbits and mice. IV. The fate of S35-sulfanil-azo-sheep stromata in X-irradiated, immunized or splenectomized rabbits. V. A subfraction from rabbit liver mitochondria which retains a high concentration of radioactivity from S35-sulfanil-azo-protein. J. infect. Dis. 96, 105, 118, 129 (1955).

    PubMed  CAS  Google Scholar 

  • Kern, M., E. Helmreich and H. N. Eisen: A demonstration of antibody activity on microsomes. Proc. nat. Acad. Sci. 45, 862 (1959).

    PubMed  CAS  Google Scholar 

  • Keston, A., and J.C. Dreyfus: Tracer studies in protein synthesis: antibody formation by spleen slices. Fed. Proc. 10, 206 (1951).

    Google Scholar 

  • Keston, A., and B. Katchen: Incorporation of glycine-2-C14into homologous antibody by rabbit tissue slices. J. Immunol. 76, 253 (1956).

    PubMed  CAS  Google Scholar 

  • Knox, W. E., and F. C. Endicott: I131as an antigen label in the circulating serum of nonimmune rabbits. J. Immunol. 65, 523 (1950).

    PubMed  CAS  Google Scholar 

  • Korngold, L., and D. Pressman: The in-vitro purification of tissue localizing antibodies. J. Immunol. 71, 1 (1953).

    PubMed  CAS  Google Scholar 

  • Korngold, L., G. L. Stahly, M. C. Dodd and W. G. Myers : The comparative retention of antigen in the skin of immune and normal rabbits as determined with egg albumin labelled with radioactive iodine. J. Immunol. 70, 345 (1953).

    PubMed  CAS  Google Scholar 

  • Koshland, M. E.: Mechanism of antibody formation. I. Fate of I131-labeled diphtheria toxoid at the site of antibody formation. J. Immunol. 79, 162 (1957).

    PubMed  CAS  Google Scholar 

  • Kuhns, W. J., S. P. Masouredis and L. Swabey : Characterization of complexes which contain diphtheria toxin and human nonprecipitating antitoxin. J. Immunol. 82, 226 (1959).

    PubMed  CAS  Google Scholar 

  • Latta, H. : Experimental hypersensitivity in the rabbit blood and tissue concentrations of foreign proteins labeled with radioactive iodine and injected intravenously. J. Immunol. 66, 635 (1951).

    PubMed  CAS  Google Scholar 

  • Laws, J. O. : The degradation of proteins labelled with radioactive iodine in control and sensitized rabbits. Brit. J. exp. Path. 33, 354 (1952).

    PubMed  CAS  Google Scholar 

  • Laws, J. O. and G. P. Wright: The disposal and organ-distribution of radioiodinated bovine serum proteins in control and specificallγ-sensitized rabbits. Brit. J. exp. Path. 33, 343 (1952).

    PubMed  CAS  Google Scholar 

  • Masouredis, S. P. : Behavior of intravenously administered I131diphtheria toxin in the guinea pig. J. Immunol. 82, 319 (1959).

    PubMed  CAS  Google Scholar 

  • Masouredis, S. P. and M. L. Beeckmans : Comparative behavior of I131and C14labelled albumin in plasma of man. Proc. Soc. exp. Biol. (N.Y.) 89, 398 (1955).

    PubMed  CAS  Google Scholar 

  • Masouredis, S. P. : L. R. Melcher and D. C. Koblich: Specificity of radioiodinated (I131) immune globulin as determined by quantitative precipitin reaction. J. Immunol. 66, 297 (1951).

    PubMed  CAS  Google Scholar 

  • Masouredis, S. P. : L. R. Melcher and D. C. Koblich: and P. Miller : Behavior of Iodide131in guinea pigs and of I131in rabbit globulin in guinea pigs and rabbits. Amer. J. Physiol. 172, 565 (1953).

    PubMed  CAS  Google Scholar 

  • Masouredis, S. P. : L. R. Melcher and D. C. Koblich: and M. B. Shimkin: The effect of antigen administration on the behavior of I131labelled rabbit anti-ovalbumin in mice. J. Immunol. 71, 268 (1953).

    PubMed  CAS  Google Scholar 

  • Mayer, M. M., L. Levine, H. J. Rapp and A. A. Marucci: Kinetic studies on immune hemolysis. VII. Decay of EAC’1, 4, 2fixation of C’3and other factors influencing the hemolytic action of complement. J. Immunol. 73, 443 (1954).

    PubMed  CAS  Google Scholar 

  • McFarlane, A. S. : Labelling of plasma proteins with radioactive iodine. Biochem. J. 62, 135 (1956).

    PubMed  CAS  Google Scholar 

  • Melcher, R. L., and S. P. Masouredis: The in vivo stability of the I131protein label of rabbit antibody in guinea pigs as determined by the quantitative precipitin reaction. J. Immunol. 67, 393 (1951).

    PubMed  CAS  Google Scholar 

  • Miller, L. L., and W. F. Bale: Synthesis of all plasma protein fractions except gamma globulins by the liver. J. exp. Med. 99, 125 (1954).

    PubMed  CAS  Google Scholar 

  • Obermayer, F., and E. P. Pick: Über die chemischen Grundlagen der Arteigenschaften der Eiweißkörper. Bildung von Immunpräzipitinen durch chemisch veränderte Eiweißkörper. Wien. klin. Wschr. 19, 327 (1906).

    Google Scholar 

  • Ogata, K., M. Ogata, Y. Mochizuki and T. Nishiyama: The in vitro incorporation of carbon14-glycine into antibody and other protein fractions by popliteal lymph nodes of rabbits following the local injection of crystalline albumin. J. Biochem. (Tokyo) 43, 653 (1956).

    CAS  Google Scholar 

  • Patras, B. : Studies on the nature of the secondary immunological response. Ph.D. thesis, Indiana University 1958, 88 pp.

    Google Scholar 

  • Penn, N. W., F. Haurowitz and M. Yenson: Interaction between internally labeled complement and specific precipitates. J. Immunol. 78, 409 (1957).

    PubMed  CAS  Google Scholar 

  • Patras, B. S. Mandeles, and H. S. Anker: On the kinetics of turnover of serum albumin. Biochim. biophys. Acta 26, 349 (1957).

    Google Scholar 

  • Pressman, D., E. D. Day and M. Blau: The use of paired labeling in the determination of tumor-localizing antibodies. Cancer Res. 17, 845 (1957).

    PubMed  CAS  Google Scholar 

  • Pressman, D. H. N. Eisen, M. Siegel, P. J. Fitzgerald, B. Sherman and A. N. Silverstein: The zone of localization of antibodies. X. The use of radioactive sulfur35as a label for anti-kidney serum. J. Immunol. 65, 559 (1950).

    PubMed  CAS  Google Scholar 

  • Pressman, D., and B. Sherman: The in vivo purification of kidneγ-localizing anti-kidney antibody. J. Immunol. 67, 15 (1951).

    PubMed  CAS  Google Scholar 

  • Pressman, D., and L. A. Sternberger: The nature of the combining sites of antibodies. The specific protection of the combining site by hapten during iodination. J. Immunol. 66, 609 (1951).

    PubMed  CAS  Google Scholar 

  • Rajam, P. C., and A. L. Jackson: In vitrolabelling of antibody globulin by tritium exchange. Nature (Lond.) 184, 375 (1959).

    PubMed  CAS  Google Scholar 

  • Rajam, P. C. and C. T. Knorp: A method for radioiodination of antibody protein. J. Lab. clin. Med. 49, 128 (1957).

    PubMed  CAS  Google Scholar 

  • Ranney, H. M., and I. M. London: Antibody formation in surviving tissues. Fed. Proc. 10, 562 (1951).

    PubMed  CAS  Google Scholar 

  • Richter, M., and F. Haurowitz: Incorporation of amino acids into antibody during the secondary response. J. Immunol. 84, 123 (1960a).

    CAS  Google Scholar 

  • Richter, M., and F. Haurowitz: Continuous synthesis of antibody after primary immunization with protein antigens. J. Immunol. 84, 420 (1960b).

    Google Scholar 

  • Schoenheimer, R., S. Ratner, D. Rittenberg and M. Heidelberger: The nitration of the blood proteins of the rat with dietary nitrogen. J. biol. Chem. 144, 541 (1942a).

    CAS  Google Scholar 

  • Schoenheimer, R., S. Ratner, D. Rittenberg and M. Heidelberger: The interaction of antibody protein with dietary nitrogen in actively immunized animals. J. biol. Chem. 144, 545 (1942b).

    CAS  Google Scholar 

  • Schwarz, R., and W. Dameschek: Drug-induced immunological tolerance. Nature (Lond.) 183, 1682 (1959).

    Google Scholar 

  • Sorkin, E., and S. V. Boyden: Studies on the fate of antigens in vitro.I. The effect of specific antibody on the fate of I131-trace labelled human serum albumin in vitroin the presence of guinea pig monocytes. J. Immunol. 82, 332 (1959).

    PubMed  CAS  Google Scholar 

  • Spar, I. L., W. F. Bale, D.E. Wolfe, R. L. Goodland and W. Dewey: A search for tissue-fixed antibodies — distribution and nature of antibodies against horse serum produced in rabbits, rats and guinea pigs. U. of Rochester AE proj. UR—484 (1957).

    Google Scholar 

  • Stark, O. K. : Studies on pneumococcal polysaccharide. II. Mechanism involved in production of „immunological paralysis” by type I pneumococcal polysaccharide. J. Immunol. 74, 130 (1955).

    PubMed  CAS  Google Scholar 

  • Stavitsky, A. B. : Antibody synthesis by homotransplanted cells and tissues. III. Mechanisms of antibody synthesis during the secondary response in the recipient animal. Brit. J. exp. Path. 39, 46 (1958).

    PubMed  CAS  Google Scholar 

  • Stevens, K. M., I. Gray and M. S. Schwartz: Catabolism of antibody and of serum albumin and globulin. Amer. J. Physiol. 175, 147 (1953).

    PubMed  CAS  Google Scholar 

  • Taliaferro, W. H., and L. G. Taliaferro: Amino acid incorporation into precipitin at different stages in the secondary response to bovine serum albumin. J. infect. Dis. 101, 252 (1957).

    PubMed  CAS  Google Scholar 

  • Taliaferro, W. H. and D. W. Talmage : Absence of amino acid incorporation into antibody during the induction period. J. infect. Dis. 97, 88 (1955).

    PubMed  CAS  Google Scholar 

  • Talmage, D.W., H.R. Baker and W. Akeson: The separation and analysis of labelled antibodies. J. infect. Dis. 94, 199 (1954).

    PubMed  CAS  Google Scholar 

  • Talmage, D.W., and F. J. Dixon : The influence of adjuvants on the elimination of soluble protein antigens and the associated antibody responses. J. infect. Dis. 93, 176 (1953).

    PubMed  CAS  Google Scholar 

  • Talmage, D.W., and F. J. Dixon, S. C. Bukantz and G. J. Dammin: Antigen elimination from the blood as an early manifestation of the immune response. J. Immunol. 67, 243 (1951).

    PubMed  CAS  Google Scholar 

  • Talmage, D.W. and G. G. Fretter: The blocking of labelled antibody uptake as a measure of the relative combining capacity of anti-red cell serums. J. infect. Dis. 98, 277 (1956).

    PubMed  CAS  Google Scholar 

  • Talmage, D.W. O. Rampersad and A. Moyer: A criterion of homogeneity in radioactively labelled antigens. Fed. Proc. 18, 600 (1959).

    Google Scholar 

  • Tarver, H., M. Tabachnick, E. S. Cannellakis, D. Fraser and H. A. Barker: Biosynthesis of C14-labeled protein and amino acids with Ehodospirillum rubrum.Arch. Biochem. 41, 1 (1952).

    CAS  Google Scholar 

  • Tekman, S., and C. E. Dalgliesh: Isotopic labelling of a specific antibody. Brit. J. exp. Path. 35, 118 (1954).

    PubMed  CAS  Google Scholar 

  • Tekman, S. and A. Ugur: Paper electrophoresis of a purified specific antibody. Nature (Lond.) 175, 594 (1955).

    CAS  Google Scholar 

  • Terres, G., and W. Wolins: Immune degradation in passively sensitized mice I. Degradation of antigen as a function of the amount of antigen and antibody used. J. Immunol. 83, 9 (1959).

    PubMed  CAS  Google Scholar 

  • Walter, H., S. Fleischer and F. Haurowitz: The metabolic fate of different external labels in doubly labelled protein antigens. Fed. Proc. 18, 602 (1959).

    Google Scholar 

  • Walter, H., and F. Haurowitz : Unpublished experiments.

    Google Scholar 

  • Walter, H., and F. Haurowitz: S. Fleischer, A. Lietze, H. F. Cheng, J. E. Turner and W. Friedberg : The metabolic fate of injected homologous serum protein in rabbits. J. biol. Chem. 224, 107 (1957).

    PubMed  CAS  Google Scholar 

  • Warren, S., and F. J. Dixon: Antigen tracer studies and histological observations in anaphylactic shock in the guinea pig. Amer. J. med. Sci. 216, 136 (1948).

    PubMed  CAS  Google Scholar 

  • Weigle, W.O., and F. J. Dixon: The elimination of heterologous serum proteins and associated antibody response in guinea pigs and rats. J. Immunol. 79, 24 (1957).

    PubMed  CAS  Google Scholar 

  • Williams, R. B., and R. M. C. Dawson : The biosynthesis of L-cystine and L-methionine labelled with radioactive sulphur (35S). Biochem. J. 52, 314 (1952).

    PubMed  CAS  Google Scholar 

  • Wormall, A. : The immunological specificity of chemically altered proteins. J. exp. Med. 51, 295 (1930).

    PubMed  CAS  Google Scholar 

  • Yenson, M. : Unpublished experiments.

    Google Scholar 

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Haurowitz, F. (1961). Use of Radioisotopes in Immunochemical Research. In: Henle, W., Kikuth, W., Meyer, K.F., Nauck, E.G., Tomcsik, J. (eds) Ergebnisse der Mikrobiologie Immunitätsforschung und Experimentellen Therapie. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-38352-0_1

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