Chemical properties of functional groups of mouse immunoglobulins of the IgA, IgG2a, and IgM classes.
暂无分享,去创建一个
[1] R. Dwek,et al. Mobility and symmetry in the Fc and pFc' fragments as probed by 1H NMR. , 1979, Molecular immunology.
[2] L. Hood,et al. Amino acid sequence of a mouse immunoglobulin mu chain. , 1979, Proceedings of the National Academy of Sciences of the United States of America.
[3] L M Amzel,et al. Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin new at 2.0 A resolution. , 1981, The Journal of biological chemistry.
[4] S. Rudikoff,et al. kappa Chain variable region from M167, a phosphorylcholine binding myeloma protein. , 1978, Biochemistry.
[5] C. Jenkin,et al. Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-sepharose. , 1978, Immunochemistry.
[6] J. Engel,et al. Selective reduction and proteolysis in the hinge region of liganded and unliganded antibodies. Identical kinetics suggest lack of major conformational change in the hinge region , 1978, European journal of immunology.
[7] H. Metzger,et al. The effect of antigen on antibodies: recent studies. , 1978, Contemporary topics in molecular immunology.
[8] J. Brown,et al. Evidence for a long-range conformational change induced by antigen binding to IgM antibody. , 1977, Proceedings of the National Academy of Sciences of the United States of America.
[9] J. Bennett,et al. Primary structure of human J chain: alignment of peptides from chemical and enzymatic hydrolyses. , 1977, Biochemistry.
[10] H. Metzger,et al. Dimeric immunoglobulin E serves as a unit signal for mast cell degranulation. , 1977, Proceedings of the National Academy of Sciences of the United States of America.
[11] E. Appella,et al. Amino acid sequence of the first 217 residues of a mouse heavy chain (MOPC 47A) with a domain deletion. , 1977, Proceedings of the National Academy of Sciences of the United States of America.
[12] R. Arnon,et al. Conformational changes and complement activation induced upon antigen binding to antibodies. , 1977, Biochemical and biophysical research communications.
[13] Y. S. Liu,et al. Complete covalent structure of a human IgA1 immunoglobulin. , 1976, Science.
[14] S. Rudikoff,et al. Size differences among immunoglobulin heavy chains from phosphorylcholine-binding proteins. , 1976, Proceedings of the National Academy of Sciences of the United States of America.
[15] D. Beale,et al. Structure and function of the constant regions of immunoglobulins , 1976, Quarterly Reviews of Biophysics.
[16] B. Barger,et al. Physico-chemical characterization of murine J chain. , 1976, Immunochemistry.
[17] J. Schlessinger,et al. Conformational changes induced in a homogeneous anti-type III pneumococcal antibody by oligosaccharides of increasing size. , 1975, Biochemistry.
[18] J. Brown,et al. Activation of antibody Fc function by antigen-induced conformational changes. , 1975, Proceedings of the National Academy of Sciences of the United States of America.
[19] R. Duggleby,et al. A competitive labeling method for the determination of the chemical properties of solitary functional groups in proteins. , 1975, Biochemistry.
[20] W. Cruickshank,et al. Properties of the histidine residues of indole-chymotrypsin. Implications for the activation process and catalytic mechanism. , 1975, The Biochemical journal.
[21] M. Fougereau,et al. Determination of the primary structure of a mouse IgG2a immunoglobulin:amino-acid sequence of the Fc fragment. Implications for the evolution of immunoglobulin structure and function. , 1974, European journal of biochemistry.
[22] L. Hood,et al. Amino-acid sequence of the variable region of the heavy (alpha) chain of a mouse myeloma protein with anti-hapten activity. , 1974, Proceedings of the National Academy of Sciences of the United States of America.
[23] A. Arnone. X-ray Studies of the Interaction of CO2 with Human Deoxyhaemoglobin , 1974, Nature.
[24] E. Kabat,et al. IMMUNOCHEMICAL STUDIES ON MOUSE MYELOMA PROTEINS REACTIVE WITH DEXTRANS OR WITH FRUCTOSANS AND ON HUMAN ANTILEVANS , 1974, The Journal of experimental medicine.
[25] M. Cohn,et al. IMMUNOCHEMICAL ANALYSIS OF THE IDIOTYPES OF MOUSE MYELOMA PROTEINS WITH SPECIFICITY FOR LEVAN OR DEXTRAN , 1974, The Journal of experimental medicine.
[26] P. Jackson,et al. The hapten-binding region of protein 460. Sequence of a sulfhydryl-containing heavy chain peptide which affects menadione binding. , 1974, Journal of immunology.
[27] H. Metzger,et al. Effect of antigen binding on the properties of antibody. , 1974, Advances in immunology.
[28] E. Appella,et al. Structural studies of a heavy chain from a mouse immunoglobulin M with antibody activity. , 1973, The Journal of biological chemistry.
[29] R. Schrohenloher,et al. Use of dextran conjugated columns for the isolation of large quantities of MOPC 104E IgM. , 1972, Immunochemistry.
[30] W. Konigsberg,et al. Contact regions for dinitrophenyl and menadione haptens in an immunoglobulin binding more than one antigen. , 1972, Proceedings of the National Academy of Sciences of the United States of America.
[31] B. Chesebro,et al. Affinity labeling of a phosphorylcholine binding mouse myeloma protein. , 1972, Biochemistry.
[32] B. Hartley,et al. Competitive labelling, a method for determining the reactivity of individual groups in proteins. The amino groups of porcine elastase. , 1971, The Biochemical journal.
[33] N. Young,et al. Specificity for phosphorylcholine of six murine myeloma proteins reactive with Pneumococcus C polysaccharide and beta-lipoprotein. , 1971, Biochemistry.
[34] E. Appella. Amino acid sequences of two mouse immunoglobulin lambda chains. , 1971, Proceedings of the National Academy of Sciences of the United States of America.
[35] M. Potter,et al. Antigen-binding myeloma proteins in mice. , 1971, Annals of the New York Academy of Sciences.
[36] M. A. León,et al. Immunochemical studies of the reaction between a mouse myeloma macroglobulin and dextrans. , 1970, Biochemistry.
[37] H. Grey,et al. Studies on the structure of mouse gamma-A myeloma proteins. , 1968, Biochemistry.
[38] B. Matthews,et al. Three-dimensional Structure of Tosyl-α-chymotrypsin , 1967, Nature.
[39] W. Gray,et al. Mechanism of Antibody Synthesis: Size Differences between Mouse Kappa Chains , 1967, Science.