The Binding of Thyrotropin to Isolated Bovine Thyroid Plasma Membranes
Plasma membranes have been prepared from bovine thyroid cells and have been characterized as being reasonably free of other subcellular structures by electron microscopy and enzyme marker analysis. Bovine thyrotropin specifically binds to these membranes, and this binding can be correlated with aden...
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| Veröffentlicht in: | The Journal of biological chemistry 1973-06, Vol.248 (11), p.4092-4100 |
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| container_title | The Journal of biological chemistry |
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| creator | Amir, S M Carraway, Jr, T F Kohn, L D Winand, R J |
| description | Plasma membranes have been prepared from bovine thyroid cells and have been characterized as being reasonably free of other
subcellular structures by electron microscopy and enzyme marker analysis. Bovine thyrotropin specifically binds to these membranes,
and this binding can be correlated with adenylate cyclase activation. The binding of thyrotropin to the membranes is immediate,
is inversely dependent on temperature, is inhibited by increasing salt concentrations, and is not affected by a range of mono-,
di-, and trisaccharides. The thyroid-stimulating activity of the thyrotropin preparations is unaffected by incubation with
membranes under conditions of the binding assay.
Both the α and the β subunits of bovine thyrotropin bind to thyroid membranes, β better than α on a molar basis; only the
β subunit, however, inhibits thyrotropin binding at the concentrations tested. Mouse tumor thyrotropin is a potent inhibitor
of bovine thyrotropin binding; human thyrotropin is not as effective. Since γ-globulin preparations with or without long acting
thyroid-stimulating activity inhibit thyrotropin binding only slightly at high γ-globulin concentrations, the long acting
thyroid stimulator itself appears to have no effect on thyrotropin binding to thyroid membranes. |
| doi_str_mv | 10.1016/S0021-9258(19)43843-X |
| format | Article |
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subcellular structures by electron microscopy and enzyme marker analysis. Bovine thyrotropin specifically binds to these membranes,
and this binding can be correlated with adenylate cyclase activation. The binding of thyrotropin to the membranes is immediate,
is inversely dependent on temperature, is inhibited by increasing salt concentrations, and is not affected by a range of mono-,
di-, and trisaccharides. The thyroid-stimulating activity of the thyrotropin preparations is unaffected by incubation with
membranes under conditions of the binding assay.
Both the α and the β subunits of bovine thyrotropin bind to thyroid membranes, β better than α on a molar basis; only the
β subunit, however, inhibits thyrotropin binding at the concentrations tested. Mouse tumor thyrotropin is a potent inhibitor
of bovine thyrotropin binding; human thyrotropin is not as effective. Since γ-globulin preparations with or without long acting
thyroid-stimulating activity inhibit thyrotropin binding only slightly at high γ-globulin concentrations, the long acting
thyroid stimulator itself appears to have no effect on thyrotropin binding to thyroid membranes.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)43843-X</identifier><identifier>PMID: 4122527</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenylyl Cyclases - metabolism ; Animals ; Biological Assay ; Carbohydrates - pharmacology ; Cattle ; Cell Membrane - drug effects ; Cell Membrane - enzymology ; Cell Membrane - metabolism ; Enzyme Activation ; gamma-Globulins - pharmacology ; Long-Acting Thyroid Stimulator - pharmacology ; Microscopy, Electron ; Osmolar Concentration ; Phosphorus Isotopes ; Protein Binding ; Receptors, Cell Surface ; Temperature ; Thyroid Gland - cytology ; Thyroid Gland - drug effects ; Thyroid Gland - enzymology ; Thyroid Gland - metabolism ; Thyrotropin - antagonists & inhibitors ; Thyrotropin - metabolism ; Thyrotropin - pharmacology ; Tritium</subject><ispartof>The Journal of biological chemistry, 1973-06, Vol.248 (11), p.4092-4100</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c379t-9a3826b80015c474c7608d8329e49a07d890aa8d1ff8dc260d445f9b17c3cfad3</citedby><cites>FETCH-LOGICAL-c379t-9a3826b80015c474c7608d8329e49a07d890aa8d1ff8dc260d445f9b17c3cfad3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4122527$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Amir, S M</creatorcontrib><creatorcontrib>Carraway, Jr, T F</creatorcontrib><creatorcontrib>Kohn, L D</creatorcontrib><creatorcontrib>Winand, R J</creatorcontrib><title>The Binding of Thyrotropin to Isolated Bovine Thyroid Plasma Membranes</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Plasma membranes have been prepared from bovine thyroid cells and have been characterized as being reasonably free of other
subcellular structures by electron microscopy and enzyme marker analysis. Bovine thyrotropin specifically binds to these membranes,
and this binding can be correlated with adenylate cyclase activation. The binding of thyrotropin to the membranes is immediate,
is inversely dependent on temperature, is inhibited by increasing salt concentrations, and is not affected by a range of mono-,
di-, and trisaccharides. The thyroid-stimulating activity of the thyrotropin preparations is unaffected by incubation with
membranes under conditions of the binding assay.
Both the α and the β subunits of bovine thyrotropin bind to thyroid membranes, β better than α on a molar basis; only the
β subunit, however, inhibits thyrotropin binding at the concentrations tested. Mouse tumor thyrotropin is a potent inhibitor
of bovine thyrotropin binding; human thyrotropin is not as effective. Since γ-globulin preparations with or without long acting
thyroid-stimulating activity inhibit thyrotropin binding only slightly at high γ-globulin concentrations, the long acting
thyroid stimulator itself appears to have no effect on thyrotropin binding to thyroid membranes.</description><subject>Adenylyl Cyclases - metabolism</subject><subject>Animals</subject><subject>Biological Assay</subject><subject>Carbohydrates - pharmacology</subject><subject>Cattle</subject><subject>Cell Membrane - drug effects</subject><subject>Cell Membrane - enzymology</subject><subject>Cell Membrane - metabolism</subject><subject>Enzyme Activation</subject><subject>gamma-Globulins - pharmacology</subject><subject>Long-Acting Thyroid Stimulator - pharmacology</subject><subject>Microscopy, Electron</subject><subject>Osmolar Concentration</subject><subject>Phosphorus Isotopes</subject><subject>Protein Binding</subject><subject>Receptors, Cell Surface</subject><subject>Temperature</subject><subject>Thyroid Gland - cytology</subject><subject>Thyroid Gland - drug effects</subject><subject>Thyroid Gland - enzymology</subject><subject>Thyroid Gland - metabolism</subject><subject>Thyrotropin - antagonists & inhibitors</subject><subject>Thyrotropin - metabolism</subject><subject>Thyrotropin - pharmacology</subject><subject>Tritium</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kF1LwzAUhoMoc378hEFBEL2o5iRpm1yqOB1MFJywu5Am6Rppm5l0iv_e6obn5ly8H-fwIDQBfAUY8utXjAmkgmT8AsQlo5zRdLmHxoA5TWkGy300_rccoqMY3_EwTMAIjRgQkpFijKaL2ia3rjOuWyW-Shb1d_B98GvXJb1PZtE3qrcmufWfrrNb2ZnkpVGxVcmTbcugOhtP0EGlmmhPd_sYvU3vF3eP6fz5YXZ3M081LUSfCkU5yUuOMWSaFUwXOeaGUyIsEwoXhgusFDdQVdxokmPDWFaJEgpNdaUMPUbn29518B8bG3vZuqht0wxP-E2UHAQQnsNgzLZGHXyMwVZyHVyrwrcELH_5yT9-8heOBCH_-MnlkJvsDmzK1pr_1A7YoJ9t9dqt6i8XrCyd17VtJWFDEUiGBaE_qT12Zw</recordid><startdate>19730610</startdate><enddate>19730610</enddate><creator>Amir, S M</creator><creator>Carraway, Jr, T F</creator><creator>Kohn, L D</creator><creator>Winand, R J</creator><general>American Society for Biochemistry and Molecular Biology</general><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>19730610</creationdate><title>The Binding of Thyrotropin to Isolated Bovine Thyroid Plasma Membranes</title><author>Amir, S M ; Carraway, Jr, T F ; Kohn, L D ; Winand, R J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-9a3826b80015c474c7608d8329e49a07d890aa8d1ff8dc260d445f9b17c3cfad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Adenylyl Cyclases - metabolism</topic><topic>Animals</topic><topic>Biological Assay</topic><topic>Carbohydrates - pharmacology</topic><topic>Cattle</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - enzymology</topic><topic>Cell Membrane - metabolism</topic><topic>Enzyme Activation</topic><topic>gamma-Globulins - pharmacology</topic><topic>Long-Acting Thyroid Stimulator - pharmacology</topic><topic>Microscopy, Electron</topic><topic>Osmolar Concentration</topic><topic>Phosphorus Isotopes</topic><topic>Protein Binding</topic><topic>Receptors, Cell Surface</topic><topic>Temperature</topic><topic>Thyroid Gland - cytology</topic><topic>Thyroid Gland - drug effects</topic><topic>Thyroid Gland - enzymology</topic><topic>Thyroid Gland - metabolism</topic><topic>Thyrotropin - antagonists & inhibitors</topic><topic>Thyrotropin - metabolism</topic><topic>Thyrotropin - pharmacology</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Amir, S M</creatorcontrib><creatorcontrib>Carraway, Jr, T F</creatorcontrib><creatorcontrib>Kohn, L D</creatorcontrib><creatorcontrib>Winand, R J</creatorcontrib><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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Amir, S M</au><au>Carraway, Jr, T F</au><au>Kohn, L D</au><au>Winand, R J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Binding of Thyrotropin to Isolated Bovine Thyroid Plasma Membranes</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1973-06-10</date><risdate>1973</risdate><volume>248</volume><issue>11</issue><spage>4092</spage><epage>4100</epage><pages>4092-4100</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Plasma membranes have been prepared from bovine thyroid cells and have been characterized as being reasonably free of other
subcellular structures by electron microscopy and enzyme marker analysis. Bovine thyrotropin specifically binds to these membranes,
and this binding can be correlated with adenylate cyclase activation. The binding of thyrotropin to the membranes is immediate,
is inversely dependent on temperature, is inhibited by increasing salt concentrations, and is not affected by a range of mono-,
di-, and trisaccharides. The thyroid-stimulating activity of the thyrotropin preparations is unaffected by incubation with
membranes under conditions of the binding assay.
Both the α and the β subunits of bovine thyrotropin bind to thyroid membranes, β better than α on a molar basis; only the
β subunit, however, inhibits thyrotropin binding at the concentrations tested. Mouse tumor thyrotropin is a potent inhibitor
of bovine thyrotropin binding; human thyrotropin is not as effective. Since γ-globulin preparations with or without long acting
thyroid-stimulating activity inhibit thyrotropin binding only slightly at high γ-globulin concentrations, the long acting
thyroid stimulator itself appears to have no effect on thyrotropin binding to thyroid membranes.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>4122527</pmid><doi>10.1016/S0021-9258(19)43843-X</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | The Journal of biological chemistry, 1973-06, Vol.248 (11), p.4092-4100 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81912861 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adenylyl Cyclases - metabolism Animals Biological Assay Carbohydrates - pharmacology Cattle Cell Membrane - drug effects Cell Membrane - enzymology Cell Membrane - metabolism Enzyme Activation gamma-Globulins - pharmacology Long-Acting Thyroid Stimulator - pharmacology Microscopy, Electron Osmolar Concentration Phosphorus Isotopes Protein Binding Receptors, Cell Surface Temperature Thyroid Gland - cytology Thyroid Gland - drug effects Thyroid Gland - enzymology Thyroid Gland - metabolism Thyrotropin - antagonists & inhibitors Thyrotropin - metabolism Thyrotropin - pharmacology Tritium |
| title | The Binding of Thyrotropin to Isolated Bovine Thyroid Plasma Membranes |
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