Water soluble guinea pig transplantation antigen from carcinogen-induced sarcomas.
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Animals↗
Biomedical subjects
R A Reisfeld
Publications and source records attributed to R A Reisfeld.
Isolation and chemical properties of porcine thyrocalcitonin.
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Amino Acids↗
Chemical and immunochemical characterization of electrophoretic subfractions of rabbit gammaG-immunoglobulin light chains with b4 allotypic specificity.
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Alanine↗
Chemical and immunochemical evidence for different classes of rabbit light polypeptide chains.
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Amino Acids↗
Water-soluble human transplantation antigen.
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Adult↗
The association of the c7 allotype of rabbits with some light polypeptide chains which lack b locus allotypy.
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Animals↗
Direct demonstration and quantitatin of Aal, Aa2 and Aa3 allotypic specificities on Fd-fragments of rabbit immunoglobulin G.
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Alleles↗
Differences in the amino acid compositions of allogeneic guinea pig transplantation antigens.
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Alanine↗
Chemical properties of porcine thyrocalcitonin.
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Amino Acids↗
A procedure for rapid and sensitive staining of protein fractionated by polyacrylamide gel electrophoresis.
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Acrylic Resins↗
Purification of porcine thyrocalcitonin.
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Acrylic Resins↗
Electrophoretic purification of a water-soluble guinea pig transplantation antigen.
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Acrylic Resins↗
Isolation and characterization of a mitogen from pokeweek (Phytolacca americana).
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Acrylic Resins↗
Electrophoretic heterogeneity of the polypeptide chains of human G-myeloma proteins.
The light and heavy polypeptide chains derived from human Gmyeloma proteins are electrophoretically heterogeneous as judged by disc electrophoresis of the polypeptide chains in urea-acrylamide gels. Individual myeloma proteins contained as many as eight light-chain and nine heavy-chain components.
Blood Protein Electrophoresis↗
Electrophoretic heterogeneity of polypeptide chains of specific antibodies.
Heavy and light polypeptide chains isolated from different specific antibodies to haptens and from (gamma)G-immunoglobulin of normal rabbits have been resolved into distinct, multiple components by disc electrophoresis in polyacrylamide gels in the presence of urea. In spite of the resolution of these chains into multiple bands, different specific antibodies and normal rabbit (gamma)G-immunoglobulin were indistinguishable from each other by this method.
Animals↗
An evaluation of the number of b4 allotypic determinants on rabbit gamma-G-immunoglobulin using double-labeled, soluble complexes with univalent antibody fragments.
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Animals↗
Peptide maps of rabbit gamma-G-immunoglobulin heavy chains controlled by allelic genes.
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Animals↗