Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Robert W. Rosenstein"'
Publikováno v:
Immunology today. 3(4)
Publikováno v:
Science. 187:130-137
Publikováno v:
Molecular Immunology. 16:657-664
Sera directed against the public and private idiotypic determinants of protein 460 and protein 315 were used to detect the presence of these idiotypic markers in serum immunoglobulins of various inbred mouse strains. Private protein 315 determinants
Publikováno v:
Molecular Immunology. 16:361-370
The preparation and characterization of rabbit antibodies directed against structures associated with thehapten binding site of proteins 315 and 460 is described. That these antibodies are site-directed was shown by: (a) specific elution of anti-idio
Publikováno v:
The Journal of Immunology. 120:886-894
Hapten-specific delayed time course skin reactions containing predominant accumulations of basophils and eosinophils were elicited in newborn guinea pigs after i.v. transfer of small amounts of oxazolone immune serum. The immune serum was fractionate
Publikováno v:
Immunochemistry. 13:939-943
Proteins 315 and 460 are IgA 2 mouse myeloma immunoglobulins which bind the haptens 2,4-Dnp and Menadione, and their derivatives competitively in the combining region. We have studied the binding of these proteins to a series of Dnp and Menadione bas
Publikováno v:
Molecular Immunology. 16:371-378
Both myeloma protein 460 and myeloma protein 315 each exhibit two sets of idiotypic determinants. A ‘private’ determinant set which distinguishes protein 460 and protein 315 from each other, and a common or ‘public’ set of idiotypic determina
Autor:
Robert W. Rosenstein, Robert A. Musson, Frank F. Richards, William H. Konigsberg, Martine Y. K. Armstrong
Publikováno v:
Proceedings of the National Academy of Sciences. 69:877-881
Protein 460 is a mouse myeloma γ A 2 protein that competitively binds two small haptens, 2,4-ε-dinitrophenyl-L-lysine (Dnp-Lys) and 2-methyl-1:4-naphthaquinone thioglycollate (MenTG), to the antibody-combining region. The intact protein has a relat
Autor:
George Taborsky, Robert W. Rosenstein
Publikováno v:
Biochemistry. 9:649-657
Publikováno v:
The Journal of Experimental Medicine
The role of bivalence of antibody in its capacity to neutralize virus was studied with rabbit antibodies to the bacteriophage, ϕX174. Univalent Fab or Fab' fragments of IgG isolated from antiviral antisera obtained early in the immunization schedule