The Attachment of IgG to Cell Components: A Reconsideration of Brambell's Receptor Hypothesis of Protein Transmission
Nuclear, mitochondrial and microsomal fractions were prepared from rabbit yolk-sac splanchnopleur and rabbit chorio-allantoic placenta, and tested in vivo and in vitro for attachment of labelled rabbit and bovine IgG. Similar fractions were prepared from small intestinal scrapings of neonatal rats,...
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| Veröffentlicht in: | Proceedings of the Royal Society of London. Series B, Biological sciences Biological sciences, 1974-09, Vol.187 (1087), p.209-219 |
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| container_issue | 1087 |
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| container_title | Proceedings of the Royal Society of London. Series B, Biological sciences |
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| creator | Hemmings, W. A. Williams, E. W. |
| description | Nuclear, mitochondrial and microsomal fractions were prepared from rabbit yolk-sac splanchnopleur and rabbit chorio-allantoic placenta, and tested in vivo and in vitro for attachment of labelled rabbit and bovine IgG. Similar fractions were prepared from small intestinal scrapings of neonatal rats, and tested in vivo and in vitro for attachment of labelled rat and sheep IgG. In all cases the attachment of the homologous and heterologous proteins was substantially equal. Digestion experiments on the labelled organelle pellets of rabbit yolk-sac were carried out with the proteases of the macerated tissue (the cell sap or final supernatant) at optimum pH. The nuclear pellet gave rise to a higher proportion of breakdown products derived from bovine than from rabbit IgG, showing the existence of a mechanism whereby selection between the two proteins might be brought about. |
| doi_str_mv | 10.1098/rspb.1974.0070 |
| format | Article |
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A. ; Williams, E. W.</creator><creatorcontrib>Hemmings, W. A. ; Williams, E. W.</creatorcontrib><description>Nuclear, mitochondrial and microsomal fractions were prepared from rabbit yolk-sac splanchnopleur and rabbit chorio-allantoic placenta, and tested in vivo and in vitro for attachment of labelled rabbit and bovine IgG. Similar fractions were prepared from small intestinal scrapings of neonatal rats, and tested in vivo and in vitro for attachment of labelled rat and sheep IgG. In all cases the attachment of the homologous and heterologous proteins was substantially equal. Digestion experiments on the labelled organelle pellets of rabbit yolk-sac were carried out with the proteases of the macerated tissue (the cell sap or final supernatant) at optimum pH. 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A.</creatorcontrib><creatorcontrib>Williams, E. W.</creatorcontrib><title>The Attachment of IgG to Cell Components: A Reconsideration of Brambell's Receptor Hypothesis of Protein Transmission</title><title>Proceedings of the Royal Society of London. Series B, Biological sciences</title><addtitle>Proc. R. Soc. Lond. B</addtitle><addtitle>Proc. R. Soc. Lond. B</addtitle><description>Nuclear, mitochondrial and microsomal fractions were prepared from rabbit yolk-sac splanchnopleur and rabbit chorio-allantoic placenta, and tested in vivo and in vitro for attachment of labelled rabbit and bovine IgG. Similar fractions were prepared from small intestinal scrapings of neonatal rats, and tested in vivo and in vitro for attachment of labelled rat and sheep IgG. In all cases the attachment of the homologous and heterologous proteins was substantially equal. Digestion experiments on the labelled organelle pellets of rabbit yolk-sac were carried out with the proteases of the macerated tissue (the cell sap or final supernatant) at optimum pH. The nuclear pellet gave rise to a higher proportion of breakdown products derived from bovine than from rabbit IgG, showing the existence of a mechanism whereby selection between the two proteins might be brought about.</description><subject>Animals</subject><subject>Binding Sites, Antibody</subject><subject>Cattle</subject><subject>Cell Fractionation</subject><subject>Cell Membrane - immunology</subject><subject>Cell nucleus</subject><subject>Cell Nucleus - immunology</subject><subject>Endoderm - immunology</subject><subject>Epithelial Cells</subject><subject>Epithelium - immunology</subject><subject>Female</subject><subject>Fractions</subject><subject>Glycocalyx</subject><subject>Immunoglobulin G</subject><subject>Microsomes - immunology</subject><subject>Mitochondria - immunology</subject><subject>Pinocytosis</subject><subject>Placenta</subject><subject>Placenta - immunology</subject><subject>Placenta - ultrastructure</subject><subject>Pregnancy</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Receptors</subject><subject>Sheep</subject><subject>Sheep - immunology</subject><subject>Ungulates</subject><subject>Vitelline Membrane - immunology</subject><subject>Vitelline Membrane - ultrastructure</subject><issn>0962-8452</issn><issn>0080-4649</issn><issn>0950-1193</issn><issn>1471-2954</issn><issn>2053-9193</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9ks2P0zAQxSMEWsrClQMSUk5wSvFnbHNB3Qq2K1awlLJXy0mdrUsTB9sBwl-P01SVKsSeLOv95s3Ms5PkOQRTCAR_43xbTKFgZAoAAw-SCSQMZkhQ8jCZAJGjjBOKHidPvN8CAATl9Cw5I5DiHLFJ0q02Op2FoMpNrZuQ2iq9urtMg03nerdL57ZubRMF_zadpUtd2sabtXYqGNsM8IVTdRHJ135QdRusSxd9a8NGe-MH4sbZoE2TrpxqfG28j5VPk0eV2nn97HCeJ98-vF_NF9n158ur-ew6K6lgIVOEMk7XpOCAiyrHiOuKl4qWmMAK8ZwKVGBQIVbktMCqpJVWUYJ4rQVQSuDz5NXo2zr7o9M-yDhAGcdVjbadlxzFGBjOIzgdwdJZ752uZOtMrVwvIZBDznLIWQ45yyHnWPDy4NwVtV4f8UOwUcej7mwfN7Sl0aGXW9u5Jl7_7-rvq1p-vbmAgoqfkDMDAWcScAxBjnOI5B_T7u0GQEZAxqg7LffYaZt_u74Yu259fL7jKiwnhEYxG0Xjg_59FJX7LmNyjMpbTiRbLlafwJeP8jby70Z-Y-42v4zT8mSXfev4i0L8U_sp9_MhIGTV7XayXVfRAd7rYPvW-eKkGP8FTfzw3g</recordid><startdate>19740917</startdate><enddate>19740917</enddate><creator>Hemmings, W. A.</creator><creator>Williams, E. W.</creator><general>The Royal Society</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19740917</creationdate><title>The Attachment of IgG to Cell Components: A Reconsideration of Brambell's Receptor Hypothesis of Protein Transmission</title><author>Hemmings, W. A. ; Williams, E. W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c597t-a45785d4b8089f6328ef8ca5c341f286592b30f27b65b3ac5fea34113de90aa93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>Animals</topic><topic>Binding Sites, Antibody</topic><topic>Cattle</topic><topic>Cell Fractionation</topic><topic>Cell Membrane - immunology</topic><topic>Cell nucleus</topic><topic>Cell Nucleus - immunology</topic><topic>Endoderm - immunology</topic><topic>Epithelial Cells</topic><topic>Epithelium - immunology</topic><topic>Female</topic><topic>Fractions</topic><topic>Glycocalyx</topic><topic>Immunoglobulin G</topic><topic>Microsomes - immunology</topic><topic>Mitochondria - immunology</topic><topic>Pinocytosis</topic><topic>Placenta</topic><topic>Placenta - immunology</topic><topic>Placenta - ultrastructure</topic><topic>Pregnancy</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Receptors</topic><topic>Sheep</topic><topic>Sheep - immunology</topic><topic>Ungulates</topic><topic>Vitelline Membrane - immunology</topic><topic>Vitelline Membrane - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hemmings, W. A.</creatorcontrib><creatorcontrib>Williams, E. W.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Proceedings of the Royal Society of London. Series B, Biological sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hemmings, W. A.</au><au>Williams, E. W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Attachment of IgG to Cell Components: A Reconsideration of Brambell's Receptor Hypothesis of Protein Transmission</atitle><jtitle>Proceedings of the Royal Society of London. Series B, Biological sciences</jtitle><stitle>Proc. R. Soc. Lond. B</stitle><addtitle>Proc. R. Soc. Lond. B</addtitle><date>1974-09-17</date><risdate>1974</risdate><volume>187</volume><issue>1087</issue><spage>209</spage><epage>219</epage><pages>209-219</pages><issn>0962-8452</issn><issn>0080-4649</issn><issn>0950-1193</issn><eissn>1471-2954</eissn><eissn>2053-9193</eissn><abstract>Nuclear, mitochondrial and microsomal fractions were prepared from rabbit yolk-sac splanchnopleur and rabbit chorio-allantoic placenta, and tested in vivo and in vitro for attachment of labelled rabbit and bovine IgG. Similar fractions were prepared from small intestinal scrapings of neonatal rats, and tested in vivo and in vitro for attachment of labelled rat and sheep IgG. In all cases the attachment of the homologous and heterologous proteins was substantially equal. Digestion experiments on the labelled organelle pellets of rabbit yolk-sac were carried out with the proteases of the macerated tissue (the cell sap or final supernatant) at optimum pH. The nuclear pellet gave rise to a higher proportion of breakdown products derived from bovine than from rabbit IgG, showing the existence of a mechanism whereby selection between the two proteins might be brought about.</abstract><cop>London</cop><pub>The Royal Society</pub><pmid>4153627</pmid><doi>10.1098/rspb.1974.0070</doi><tpages>11</tpages></addata></record> |
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| ispartof | Proceedings of the Royal Society of London. Series B, Biological sciences, 1974-09, Vol.187 (1087), p.209-219 |
| issn | 0962-8452 0080-4649 0950-1193 1471-2954 2053-9193 |
| language | eng |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing |
| subjects | Animals Binding Sites, Antibody Cattle Cell Fractionation Cell Membrane - immunology Cell nucleus Cell Nucleus - immunology Endoderm - immunology Epithelial Cells Epithelium - immunology Female Fractions Glycocalyx Immunoglobulin G Microsomes - immunology Mitochondria - immunology Pinocytosis Placenta Placenta - immunology Placenta - ultrastructure Pregnancy Rabbits Rats Receptors Sheep Sheep - immunology Ungulates Vitelline Membrane - immunology Vitelline Membrane - ultrastructure |
| title | The Attachment of IgG to Cell Components: A Reconsideration of Brambell's Receptor Hypothesis of Protein Transmission |
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