Abstract
Virtually all cells express some capacity to recognize and respond to external molecular stimuli. One system that has been subjected to extensive study is the recognition of an antigen by immunologically competent lymphocytes. This is a phenomenon in which cell-surface receptor molecules bind “non-self” ligands in a specific manner. This binding initiates a chain of molecular events that underlie lymphocyte activation and interaction among immunocytes, with the eventual results being the production of specific effector thymus-derived (T) or bonemarrow-derived (B) cells. The capacity to discriminate between “self” and “nonself” is not restricted to vertebrate species, although the receptors and mechanisms evolved by plants (Clarke and Knox, 1978) and invertebrate species (Jenkin, 1976) apparently differ from those of the vertebrate immune system (Marchalonis, 1977 a). Available data suggest that surface glycoproteins are involved in such recognition events, and the possible similarities and differences governing cell-surface recognition in these three systems and in embryonic development are problems of great current interest.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Acton, R. T., Bennett, J. C., Evans, E. E., and Schrohenloher, R. E., 1969, Physical and chemical characterization of oyster hemagglutinin, J. Biol. Chem. 244: 4128.
Ahmann, G. B., and Sage, H. J., 1974, Binding of purified lectins to guinea pig lymphocytes, Cell. Immunol. 13: 407.
Ambrosius, H., and Fiebig, H., 1972, Evolution of antibody affinity, in: L’Étude Phylogénique et Ontogénique de la Résponse Immunitaire et son Apport à la Théorie Immunologique (P. Liacopoulos and J. Panijel, eds.), pp. 135–146, Inserm, Boulogne.
Appella, E., 1971, Amino acid sequence of two mouse Immunoglobulin lambda chains, Proc. Natl. Acad. Sci. USA 68: 590.
Balsamo, J., and Lilien, J., 1975, The binding of tissue specific adhesive molecules to the cell surface. A molecular basis for specificity, Biochemistry 14: 167.
Becker, J. W., Reeke, G. N., Jr., and Edelman, G. M., 1971, Location of the saccharide binding site of concanavalin A, J. Biol. Chem. 246: 6123.
Benacerraf, B., 1978, A hypothesis to relate the specificity of T lymphocytes and the activity of I region-specific Ir genes in macrophages and B lymphocytes, J. Immunol. 120: 1809.
Berken, A., and Benacerraf, B., 1966, Properties of antibodies cytophilic for macrophages, J. Exp. Med. 123: 119.
Bernard, C. C. A., Roberts, I. M., and Mackay, I. R., 1977, Experimental autoimmune encephalomyelitis in mice antigen binding lymphocyte to basic protein of myelin insusceptible and resistance strains, J. Immunogenetics 4: 277.
Berson, S. A., and Yalow, R. S., 1959, Quantitative aspects of the reaction between insulin and insulin binding antibody, J. Clin. Invest. 38: 1996.
Binz, H., and Wigzell, H., 1978, Antigen binding, idiotypic T-lymphocyte receptors, in: Contemporary Topics in Immunobiology, Vol. 7: T Cells (O. Stutman, ed.), pp. 113–177, Plenum Press, New York.
Binz, H., Wigzell, H., and Bazin, H., 1976, T-cell idiotypes are linked to immunoglobulin heavy chain genes, Nature 264: 639.
Bluestein, H., 1974, Alloantiserum-mediated suppression of histocompatibility linked Ir-gene controlled immunoresponses, J. Exp. Med. 140: 481.
Capra, J. D., Tung, A. S., and Nisonoff, A., 1975, Structural studies on induced antibodies with defined idiotypic specificities. I. The heavy chains of anti-p-azophenylarsonate antibodies from A/J mice bearing a cross reactive idiotype, J. Immunol. 114: 1548.
Capra, J. D., Klapper, D. G., Tung, A. S., and Nisonoff, A., 1977, Identical hyperavailable regions in light chains of differing VK subgroups, Cold Spring Harbor Symp. Quant. Biol. 41: 847.
Cesari, I. M., and Weigert, M., 1973, Mouse lambda-chain sequences, Proc. Natl. Acad. Sci. USA 70: 2112.
Chothia, C., and Janin, J., 1975, Principles of protein-protein recognition, Nature 256: 705.
Clarke, A., and Knox, R. B., 1978, Cell recognition in flowering plants, Q. Rev. Biol. 53: 3.
Clem, L. W., and Small, P. A., Jr., 1967, Phylogeny of immunoglobulin structure and function, J. Exp. Med. 125: 893.
Cone, R. E., 1976, Factors influencing the isolation of membrane Immunoglobulins from T and B lymphocytes, J. Immunol. 116: 847.
Cone, R. E., 1978, The search for the T cell antigen receptor, in Progress in Immunology III, pp. 8–17, Australian Academy of Science, Canberra.
Cone, R. E., and Brown, W., 1976, Isolation of membrane associated Immunoglobulins from T lymphocytes by non-ionic detergents, Immunochemistry 13: 571.
Cone, R., and Janeway, C., 1977, The T cell receptors, in: Immune System: Genetics and Regulation (E. E. Sercarz, L. A. Herzenberg, and C. F. Fox, eds.), pp. 175–178, Academic Press, New York.
Cone, R. E., and Marchalonis, J. J., 1974, Surface proteins of thymus-derived lymphocytes and bone-marrow-derived lymphocytes: Selective isolation of immunoglobulin and the theta antigen by non-ionic detergents, Biochem. J. 140: 345.
Cone, R. E., Hoessli, D., and Rosenstein, R. W., 1977, Analysis of detergent-extracted Immunoglobulins of T and B lymphocytes by ultracentrifugation and column chromatography, Immunochemistry 14: 345.
Conrad, D. H., Bazin, H., Sehon, A. H., and Froese, A., 1975, Binding parameters of the interaction between rat IgE and rat mast cell receptors, J. Immunol. 114: 1688.
Cooper, M. D., and Dayton, D. H., 1977, Development of Host Defenses, Raven Press, New York.
Cuatrecasas, P., and Hollenberg, M. D., 1976, Membrane receptors and hormone action, Adv. Prot. Chem. 30: 251.
Cuilen, S. E., David, C. S., Shreffler, D. C., and Nathenson, S. G., 1974, Membrane molecules determined by the H-2 associated immune response region: Isolation and some properties, Proc. Natl Acad. Sci. USA 71: 648.
Cunningham, B. A., Wang, J. L., Pflumm, M. N., and Edelman, G. M., 1972, Isolation and proteolytic cleavage of the intact subunit of concanavalin A, Biochemistry 11: 3233.
Curtain, C. C., 1979, Lymphocyte surface modulation and glycosphingolipids, Immunology 36: 805.
Curtain, C. C., Looney, F. D., Marchalonis, J. J., and Raison, J. K., 1978, Changes in lipid ordering and state of aggregation in lymphocyte plasma membranes after exposure to mitogens, J. Membr. Biol. 44: 211.
Decker, J. M., and Marchalonis, J. J., 1978, Molecular events in lymphocyte activation: Role of nonhistone chromosomal proteins in regulating gene expression, in: Contemporary Topics in Molecular Immunology, Vol. 7 (R. A. Reisfeld and F. P. Inman, eds.), pp. 365–413, Plenum Press, New York.
Decker, J. M., Warr, G. W., and Marchalonis, J. J., 1977, A membrane glycoprotein which binds antilymphocyte globulin and concanavalin A is implicated in stimulation of murine T lymphocytes, Biochem. Biophys. Res. Commun. 74: 1536.
DeLuca, D., Warr, G. W., and Marchalonis, J. J., 1978, Phylogenetic origins of immune recognition: Lymphocyte surface Immunoglobulins and antigen binding in the genus Carassius (Teleostii), Eur. J. Immunol. 8: 525.
DeLuca, D., Warr, G. W., and Marchalonis, J. J., 1979, Codistribution of antigen and Fab determinants on thymic antigen-binding cells, in: Function and Structure of the Immune System (W. Müller-Ruchholtz and H. K. Müller-Hermelink, eds.), pp. 165–171, Plenum Press, New York.
Dickler, H. B., 1976, Lymphocyte receptors for Immunoglobulin, Adv. Immunol. 24: 167.
Edelman, G. M., 1972, The covalent and three dimensional structure of concanavalin A, Proc. Natl. Acad. Sci. USA 69: 2580.
Eisen, H. N., and Karush, F., 1949, The interaction of purified antibody with homologous hapten: antibody valence and binding constant, J. Am. Chem. Soc. 71: 363.
Erb., P., and Feldmann, M., 1975, The role of macrophages in the generation of helper cells. II. The genetic control of the macrophage T cell interaction for helper cell induction with soluble antigen, J. Exp. Med. 142: 460.
Feldmann, M., 1977, Cell interactions in the immune response in vitro in: The Lymphocyte: Structure and Function (J. J. Marchalonis, ed.), pp. 279–307, Marcel Dekker, New York.
Finstad, J., Good, R. A., and Litman, G. W., 1974, The erythrocyte agglutinin from Limulus polyphemus hemolymph: Molecular structure and biological function, Ann. N. Y. Acad. Sci. 234: 170.
Fishelson, Z., and Berke, G., 1978, T lymphocyte-mediated cytolysis: Dissociation of the binding and lytic mechanisms of the effector cell, J. Immunol. 120: 1121.
Flanagan, J., and Koch, G. L. E., 1978, Cross-linked surface Ig attaches to actin, Nature 273: 278.
Flier, J. S., Kahn, C. R., Jarrett, D. B., and Roth, J., 1977, The immunology of the insulin receptor, in: Immunology of Receptors (B. Cinader, ed.), pp. 477–489, Marcel Dekker, New York.
Fougereau, M., Olins, D. E., and Edelman, G. M., 1964, Reconstitution of antiphage antibodies from L and H Polypeptide chains and the formation of interspecies molecular hybrids, J. Exp. Med. 120: 349.
Frazier, W. A., Rosen, S. D., Reitherman, R. W., and Barondes, S. A., 1975, Purification and comparison of two developmentally regulated lectins from Dictyostylium discoideum, J. Biol. Chem. 250: 7714.
Furthmayr, H., 1978, Structural comparison of glycophorins and immunochemical analysis of genetic variants, Nature 271: 519.
Goding, J. W., and Layton, J. E., 1976, Antigen-induced co-capping of IgM and IgD-like receptors on murine B cells, J. Exp. Med. 144: 852.
Goodman, J. W., Fong, S., Lewis, G. K., Kamin, R., Nitecki, D. E., and der Balean, G., 1978, Antigen structure and lymphocyte activation, Immunol. Rev. 39: 36.
Gray, W. R., Dreyer, W. J., and Hood, L., 1967, Mechanism of antibody synthesis size differences between mouse kappa chains, Science 155: 465.
Greaves, M. F., Bauminger, S., and Janossy, G., 1972, Lymphocyte activation. III. Binding sites for phytomitogens on lymphocyte subpopulations, Clin. Exp. Immunol. 10: 537.
Greaves, M. F., Janossy, G., Feldmann, M., and Doenhoff, M., 1974, Polyclonal mitogens and the nature of B lymphocyte activation mechanisms, in: The Immune System: Genes, Receptors and Signals (E. E. Sercarz, A. R. Williamson, and C. F. Fox, eds.), pp. 271–297, Academic Press, New York.
Grey, H. M., Abel, C. A., Yount, W. J., and Kunkel, H. G., 1968, A subclass of human γA-globulins (γA2) which lacks the disulfide bonds linking heavy and light chains, J. Exp. Med. 128: 1223.
Hämmerling, G. J., and McDevitt, H. O., 1974, Antigen binding T and B lymphocytes. II. Studies on the inhibition of antigen-binding to T and B cells by anti-immunoglobulin and anti-H-2 sera, J. Immunol. 112: 1726.
Hämmerling, U., Mack, C., and Pickel, H. G., 1976, Immunofluorescence analysis of Ig determinants of mouse thymocytes and T cells, Immunochemistry 13: 525.
Haustein, D., and Goding, J. W., 1975, Surface immunoglobulin heavy chains of murine splenocytes and thymocytes are different, Biochem. Biophys. Res. Commun. 65: 483.
Hood, L., and Ein, D., 1968, Immunoglobulin lambda chain structure: Two genes, one polypeptide chain, Nature 220: 764.
Hunt, S., and Marchalonis, J. J., 1974, Radioiodinated lymphocyte surface glycoproteins: Concanavalin A binding proteins include surface immunoglobulin, Biochem. Biophys. Res. Commun. 61: 1227.
Jenkin, C. R., 1976, Factors involved in the recognition of foreign material by phagocytic cells from invertebrates, in: Comparative Immunology (J. J. Marchalonis, ed.), pp. 80–97, Blackwell, Oxford.
Jones, V. E., Graves, H. E., and Orlans, E., 1976, The detection of (Fab′)2-related surface antigens in the thymocytes of children, Immunology 30: 281.
Kabat, E. A., Wu, T. T., and Bilofsky, H., 1976, Variable Regions of Immunoglobulin Chains, Medical Computer Systems, Cambridge, Mass.
Karush, F., 1957, The interaction of purified anti-β-laetoside antibody with haptens, J. Am. Chem. Soc. 79: 3380.
Karush, F., 1962, Immunologic specificity and molecular structure, Adv. Immunol. 2:1.
Katz, D. H., and Benacerraf, B., 1975, The function and interrelationships of T cell receptors, Ir genes and other histocompatibility gene products, Transpl. Rev. 22: 175.
Kauzmann, W., 1959, Some factors in the interpretation of protein denaturation, Adv. Prot. Chem. 14: 1.
Kindmark, C.-O., 1971, Stimulating effect of C-reactive protein on phagocytosis of various species of pathogenic bacteria, Clin. Exp. Immunol. 8: 941.
Klein, J., 1976, An attempt at an interpretation of the mouse H-2 complex, in: Contemporary Topics in Immunobiology, Vol. 5 (W. O. Weigle, ed.), pp. 297–336, Plenum Press, New York.
Kubo, R. T., Rosenblum, I. Y., and Benedict, A. A., 1971, Amino terminal sequences of heavy and light chains of chicken anti-dinitrophenyl antibody, J. Immunol. 107: 1781.
Letarte-Muirhead, M., Barclay, A. N., and Williams, A. F., 1975, Purification of the Thy-1 molecule, a major cell surface glycoprotein of rat thymocytes, Biochem. J. 151: 685.
Li, C. H., Dixon, J. S., and Liu, W.-K., 1969, Human pituitary growth hormone, Arch. Biochem. Biophys. 133: 70.
Lis, H., and Sharon, N., 1973, The biochemistry of plant lectins (phytohemagglutinins), Ann. Rev. Biochem. 42: 541.
Loor, F., 1977, Structure and dynamics of the lymphocyte surface, in relation to differentiation, recognition and activation, Progr. Allergy 23: 1.
Mcllhinney, R. A. J., Richardson, N. E., and Feinstein, A., 1978, Evidence for a C-terminal tyrosine residue in human and mouse B-lymphocyte membrane μ-chains, Nature 272: 555.
Marchalonis, J. J., 1975, Lymphocyte surface immunoglobulin, Science 190: 20.
Marchalonis, J. J., 1976a, Surface immunoglobulin of B and T lymphocytes: Molecular properties, association with the cell membrane, in: Contemporary Topics in Molecular Immunology, Vol. 5 (H. N. Eisen and R. A. Reisfeld, eds.), pp. 125–160, Plenum Press, New York.
Marchalonis, J. J., 1976b, Isolated radioiodinated surface Immunoglobulins of murine bone marrow derived lymphocytes which bind the 2,4-dinitrophenyl hapten, Immunochemistry 13: 667.
Marchalonis, J. J., 1977a, Antigen recognition by T lymphocytes: Status of the minimal hypothesis, Ricerca 7:1.
Marchalonis, J. J., 1977b, Immunity in Evolution, Harvard University Press, Cambridge, Mass.
Marchalonis, J. J., and Cone, R. E., 1973, Biochemical and physiological properties of lymphocyte surface immunoglobulin, Transpl. Rev. 44: 3.
Marchalonis, J. J., and Edelman, G. M., 1965, Phylogenetic origins of antibody structure. I. Multichain structure of Immunoglobulins in the smooth dogfish (Mustelus canis), J. Exp. Med. 122: 601.
Marchalonis, J. J., and Edelman, G. M., 1968a, Isolation and characterization of a natural hemagglutinin from Limulus polyphemm, J. Mol. Biol. 32: 453.
Marchalonis, J. J., and Edelman, G. M., 1968b, Phylogenetic origins of antibody structure. III. Antibodies in the primary immune response of the sea lamprey, Petromyzon marinus, J. Exp. Med. 127: 891.
Marchalonis, J. J., and Moseley, J. M., 1978, The immunoglobulin-like T cell receptor problem in: Proceedings VI International Conference on Lymphatic Tissues and Germinal Centers in Immune Reactions, in press.
Marchalonis, J. J., and Warr, G. W., 1978, Phylogenetic origins of immune recognition: Naturally occurring DNP-binding molecules in cordate sera and hemolymph, J. Dev. Comp. Immunol. 2: 443.
Marchalonis, J. J., and Warr, G. W., 1979, Antigen receptors on thymus-derived lymphocytes, in: Cancer Biology Reviews, Vol. 1 (J. J. Marchalonis, M. G. Hanna, Jr., and I. J. Fidler, eds.), pp. 1–47, Marcel Dekker, New York.
Marchalonis, J. J., Morris, P. J., and Harris, A. W., 1974, Speculations on the functions of the products of immune response genes, J. Immunogenetics 1: 63.
Marchalonis, J. J., Bucana, C., Hoyer, L., Warr, G. W., Hanna, M. G., Jr., and Szenberg, A., 1978, Visualization of a guinea pig T lymphocyte surface component cross-reactive with immunoglobulin, Science 199: 433.
Marchalonis, J. J., Warr, G. W., Bucana, C., and Hoyer, L., 1979a, The immunoglobulinlike T cell receptor. I. In situ demonstration of immunoglobulin Fab-region determinants in rodent T cells, J. Immunogenet., in press.
Marchalonis, J. J., Warr, G. W., Smith, P., Begg, G. S., and Morgan, F. J., 1979b, Structural and antigenic studies of an idiotype-bearing murine antibody to the arsonate hapten, Biochemistry 18: 560.
Melcher, U., and Uhr, J. W., 1977, Density differences between membrane and secreted Immunoglobulins of murine splenocytes, Biochemistry 16: 145.
Metzger, H., 1977, Early molecular events in immunoglobulin E mediated mast cell exocytosis, in: Immune System: Genetics and Regulation (E. E. Sercarz, L. A. Herzenberg, and C. F. Fox, eds.), pp. 679–690, Academic Press, New York.
Miller, J. F. A. P., and Vadas, M. A., 1977, The major histocompatibility complex influence on immune reactivity and T-lymphocyte activation, Scand. J. Immunol. 6: 771.
Miller, J. F. A. P., Vadas, M. A., Whitelaw, A., and Gamble, J., 1976, Role of major histocompatibility complex gene products in delayed-type hypersensitivity, Proc. Natl. Acad. Sci USA 73: 2486.
Mir-Lechaire, F.-J., and Barondes, S. H., 1978, Two distinct developmentally regulated lectins in chick embryo muscle, Nature 272: 256.
Mitchell, R. E. J., Chaiken, I. M., and Smith, E. L., 1970, The complete amino acid sequence of papain, J. Biol. Chem. 245: 3485.
Moseley, J. M., Marchalonis, J. J., Harris, A. W., and Pye, J., 1977, Molecular properties of T lymphoma Immunoglobulin. I. Serological and general physicochemical properties, J. Immunogenet. 4: 233.
Moseley, J. M., Beatty, E. A., and Marchalonis, J. J., 1979b, Molecular properties of T-lymphoma Immunoglobulin. II. Peptide composition of the heavy chain, J. Immunogenet. 6: 1.
Moseley, J. M., Beatty, E. A., and Marchalonis, J. J., 1979b, Molecular properties of T-lymphoma immunoglobulin, III. Peptide composition of the light chain, J. Immunogenet. 6: 19.
Munro, A. J., and Taussig, M. J., 1975, Two genes in the major histocompatibility complex control immune responses, Nature 256: 103.
Nicolson, G. L., Poste, G., and Tae, H. J., 1977, The dynamics of cell membrane organization, in: Dynamic Aspects of Cell Surface Organization (G. Poste and G. L. Nicolson, eds.), pp. 1–73, North-Holland, Amsterdam.
Padlan, E. A., Davies, D. R., Pecht, I., Gevol, D., and Wright, D., 1977, Model-building studies of antigen binding sites: The hapten-binding site of MOPC-315, Cold Spring Harbor Symp. Quant. Biol. 41: 627.
Parker, C. W., 1974, in: Cyclic AMP, Cell Growth and the Immune Response (L. Lichtenstein and C. Parkers, eds.), p. 35, Springer-Verlag, New York.
Paul, W. E., and Benacerraf, B., 1977, Functional specificity of thymus-dependent lymphocytes, Science 195: 1293.
Perelson, A. S., 1978, Spatial distribution of surface immunoglobulin on B lymphocytes: Local ordering, Exp. Cell Res. 112: 309.
Ploegh, H. L., Orr, H. T., Robb, R., and Strominger, J. L., 1978, Structure of HLA antigens, in: Biological Markers of Neoplasia (R. Ruddon, 3d.), pp. 201–211, Plenum Press, New York.
Poljak, R. J., Amzel, L. M., Chen, B. L., Chiu, Y. Y., Phizackerley, C. K., Saul, F., and Yserum, X., 1977, Three dimensional structure and diversity of Immunoglobulins, Cold Spring Harbor Symp. Quant. Biol. 41: 639.
Poulik, M. D., 1976, in: Trace Components of Plasma: Isolation and Clinical Significance, pp. 155–177, Alan R. Liss, Inc., New York.
Putnam, F. W., Florent, G., Paul, C., Shinoda, T., and Shimizer, A., 1973, Complete amino acid sequence of the mu heavy chain of a human IgM immunoglobulin, Science 182: 287.
Raff, M. C., and Lawson, D., 1977, Membrane events in cell signalling, in: Immune System: Genetics and Regulation (E. E. Sercarz, L. A. Herzenberg, and C. F. Fox, eds.), pp. 669–678, Academic Press, New York.
Rajewsky, K., and Eichmann, D., 1977, Antigen receptors of T helper cells, in: Contemporary Topics in Immunobiology, Vol. 7: T Cells (O. Stutman, ed.), pp. 69–112, Plenum Press, New York.
Ramasamy, R., 1976, Attachment of the antigen receptor to the B cell membrane, Immunochemistry 13: 705.
Reeke, G. N., Becker, J. W., Cunningham, B. A., Gunther, G. R., Wang, J. L., and Edelman, G. M., 1974, Relationships between structure and activities of concanavalin A, Ann. N.Y. Acad. Sci. 234: 369.
Roelants, G. E., Forni, L., and Pernis, B., 1973, Blocking and redistribution (“capping”) of antigen receptors on T and B lymphocytes by anti-immunoglobulin antibody, J. Exp. Med. 137: 1060.
Roelants, G. E., Ryden, A., Hagg, L.-B. and Loor, F., 1974, Active synthesis of immunoglobulin receptors for antigen by T lymphocytes, Nature 247: 106.
Roubal, W. T., Etlinger, H. M., and Hodgins, H. O., 1974, Spin-label studies of a haptencombining site of rainbow trout antibody, J. Immunol. 113: 309.
Saul, F. A., Amzel, L. M., and Poljak, R., 1978, Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin N at 2.0 Å resolution, J. Biol. Chem. 253: 585.
Schreiner, G. F., and Unanue, E. R., 1976, Membrane and cytoplasmic changes in B lymphocytes induced by ligand-surface Immunoglobulin interaction, Adv. Immunol. 24: 37.
Schwartz, R. H., 1978, Editorial: A clonal deletion model for Ir gene control of the immune response, Scand. J. Immunol. 7: 3.
Segrest, J. P., and Feldmann, R. J., 1974, Membrane proteins: Amino acid sequence and membrane penetration, J. Mol. Biol. 87: 853.
Shearer, G. M., Schmitt-Verhulst, A.-M. and Renn, T. G., 1977, Significance of the major histocompatibility complex as assessed by T cell mediated lympholysis involving syngeneic stimulating cells, in: Contemporary Topics in Immunobiology, Vol. 7: T Cells (O. Stutman, ed.), pp. 221–243, Plenum Press, New York.
Silver, J., Cecka, J. M., McMillan, M., and Hood, L., 1977, Chemical characterization of products of the H-2 complex, Cold Spring Harbor Symp. Quant. Biol. 41: 369.
Sledge, C., Clem, L. W., and Hood, L., 1974, Antibody structure: Amino terminal sequences of nurse shark and light and heavy chains, J. Immunol. 112: 941.
Smith, S., and Revel, J. P., 1971, Mapping of concanavalin A binding sites on the surface of several cell types, Dev. Biol. 27: 434.
Smith, W. I., Ladoulis, C. T., Misra, D. N., Gell, T. J. III, and Bazin, H., 1975, Lymphocyte plasma membranes. III. Composition of lymphocyte plasma membranes of normal and immunized rats, Biochim. Biophys. Acta 382: 506.
Smyth, D. G., Stein, W. H., and Moore, S., 1963, The sequence of amino acid residues in bovine pancreatic ribonuclease revisions and confirmations, J. Biol. Chem. 238: 227.
Snary, D., Barnstable, C., Bodmer, W. F., Goodfellow, P., and Crumpton, J. J., 1977, Human Ia antigens-purification and molecular structure, Cold Spring Harbor Symp. Quant. Biol. 41: 379.
So, L. L., and Goldstein, I. J., 1968, Protein carbohydrate interaction, J. Biol. Chem. 243: 2003.
Steiner, L. A., Mikoryak, C. A., Lopes, A.D., and Green, C., 1975, Immunoglobulins in ranid frogs and tadpoles, in: Immunologic Phylogeny (W. H. Hildemann and A. A. Benedict, eds.), pp. 173–183, Plenum Press, New York.
Stockert, R. J., Morell, A. G., and Scheinberg, I. H., 1974, Mammalian hepatic lectin, Science 186: 365.
Storb, U., 1978, Direct demonstration of Immunoglobulin κ chain RNA in thymus T cells by in situ hybridization, Proc. Natl. Acad. Sci. USA 75: 2905.
Szenberg, A., Marchalonis, J. J., and Warner, N. L., 1977, Direct demonstration of endogenous murine T-cell surface immunoglobulin, Proc. Natl Acad. Sci. USA 74: 2113.
Tada, T., Taniguchi, M., and David, C. S., 1977, Suppressive and enhancing T cell factors as I-regions gene products properties and the subregion assignment, Cold Spring Harbor Symp. Quant. Biol. 41: 119.
Taylor, R. B., Duffies, P. H., Raff, M. C., and de Petris, S., 1971, Redistribution and pinocytosis of lymphocyte surface Immunoglobulin molecules induced by anti-immuoglobulin antibody, Nature New Biol. 233: 225.
Terhorst, C., Robb, R., Jones, C., and Strominger, J. L., 1977, Further structural studies of the heavy chain of HLA antigens and its similarity to Immunoglobulins, Froc. Natl. Acad. Sci. USA 74: 4002.
Titani, K., Shinoda, T., and Putnam, F. W., 1969, The amino acid sequence of a K type Bence Jones protein, J. Biol. Chem. 244: 3550.
Tung, A. J., and Nisonoff, A., 1975, Isolation from individual A/J mice of anti-p-azophenylarsonate antibodies bearing a cross-reactive idiotype, J. Exp. Med. 141: 112.
Vitetta, E. S., and Capra, J. D., 1978, The protein products of the murine 17th chromosome: Genetics and structure, Adv. Immunol. 26: 147.
Vitetta, E. S., and Uhr, J. W., 1973, Synthesis, transport, dynamics, and fate of cell surface Ig and alloantigens in murine lymphocytes, Transplant. Rev. 14: 50.
Vitetta, E. S., and Uhr, J. W., 1975, Immunoglobulin receptors revisited, Science 189: 964.
Vitetta, E. S., Bianco, C., Nussenzweig, V., and Uhr, J. W., 1972, 1972, Cell surface immunoglobulin. IV. Distribution among thymocytes, bone marrow cells, and their derived populations, J. Exp. Med. 136: 81.
Walsh, F. S., and Crumpton, M. J., 1977, Orientation of cell-surface antigens in the lipid bilayer of lymphocyte plasma membrane, Nature 269: 307.
Warner, N. L., 1974, Membrane Immunoglobulins and antigen receptors on B and T lymphocytes, Adv. Immunol. 19: 67.
Warner, N. L., and Marchalonis, J. J., 1972, Structural differences in mouse IgA myeloma proteins of different allotypes, J. Immunol. 109: 657.
Warr, G. W., and Marchalonis, J. J., 1977, Lymphocyte surface Immunoglobulins: detection, characterization and occurrence in diseases of the lymphoid system, Crit. Rev. Clin. Lab. Sciences 7: 185.
Warr, G. W., Marton, G., Szenberg, A., and Marchalonis, J. J., 1978, Reactions of chicken antibodies with immunoglobulins of mouse serum and T cells, Immunochemistry 15: 615.
Warr, G. W., DeLuca, D., and Marchalonis, J. J., 1979, The immunoglobulin-like T cell receptor. III. Binding of the arsonate hapten by idiotype-bearing T cells and antibody is blocked by avian antibody to (Fab′)2, Mol. Immunol., in press.
Yahara, I., and Edelman, G. M., 1972, Restriction of the mobility of lymphocyte Immunoglobulin receptors by concanavalin A, Proc. Natl. Acad. Sci USA 69: 608.
Yariv, J., Kalb, A. J., and Levitzki, A., 1968, The interaction of eoncanavalin A with methyl alpha-D-glucopyranoside, Biochim. Biophys. Acta 165: 303.
Zinkernagel, R. M., and Doherty, P. C., 1977, Major transplantation antigens, virsues, and specificity of surveillance T cells, in: Contemporary Topics in Immunobiology, Vol. 7: T Cells (O. Stutman, ed.), pp. 179–220, Plenum Press, New York.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1980 Plenum Press, New York
About this chapter
Cite this chapter
Marchalonis, J.J. (1980). Molecular Interactions and Recognition Specificity of Surface Receptors. In: Marchalonis, J.J., Cohen, N. (eds) Contemporary Topics in Immunobiology. Contemporary Topics in Immunobiology, vol 9. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9131-3_10
Download citation
DOI: https://doi.org/10.1007/978-1-4615-9131-3_10
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4615-9133-7
Online ISBN: 978-1-4615-9131-3
eBook Packages: Springer Book Archive