Purification and characterization of lutropin receptor from membranes of pig follicular fluid
Membranes derived from free floating granulosa cells in porcine ovarian follicular fluid were used as a starting material for structural characterization of both LH/hCG and FSH receptors. The receptors were highly hormone-specific and showed single classes of high-affinity binding sites (Kd = 19-74...
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| Veröffentlicht in: | Biochemistry (Easton) 1990-04, Vol.29 (15), p.3751-3759 |
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| creator | Yarney, T. A Sairam, M. R Bhargavi, G. N Mohapatra, S. K |
| description | Membranes derived from free floating granulosa cells in porcine ovarian follicular fluid were used as a starting material for structural characterization of both LH/hCG and FSH receptors. The receptors were highly hormone-specific and showed single classes of high-affinity binding sites (Kd = 19-74 pM). Their molecular weights as determined by affinity cross-linking with their respective 125I-ligands were similarly 70,000. The membrane-localized receptors could be solubilized with reduced Triton X-100 in the presence of 20% glycerol with good retention of hormone binding activity. The Triton extracts of membranes also showed hormone specificity and equilibrium binding constants similar to the membrane receptors (Kd = 32-48 pM). Affinity chromatography on divinylsulfonyl-Sepharose-oLH columns was utilized to purify the solubilized LH/hCG receptor to a specific activity of 2000 pmol/mg of protein. The purified receptor exhibited a high specificity for hCG and hLH but not for hFSH nor bTSH. The purified receptor was iodinated and visualized to be composed of a major protein of Mr approximately 70,000 and other minor proteins of molecular weights ranging from 14,000 to 40,000. Except for the Mr 14,000 protein, all other protein species bound to the concanavalin A-Sepharose column. The data suggest that the ovarian LH/hCG and FSH receptors are structurally similar and consist of a single polypeptide chain, as recently documented for the LH/hCG receptor (Loosefelt et al., 1989; McFarland et al., 1989). |
| doi_str_mv | 10.1021/bi00467a022 |
| format | Article |
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A ; Sairam, M. R ; Bhargavi, G. N ; Mohapatra, S. K</creator><creatorcontrib>Yarney, T. A ; Sairam, M. R ; Bhargavi, G. N ; Mohapatra, S. K</creatorcontrib><description>Membranes derived from free floating granulosa cells in porcine ovarian follicular fluid were used as a starting material for structural characterization of both LH/hCG and FSH receptors. The receptors were highly hormone-specific and showed single classes of high-affinity binding sites (Kd = 19-74 pM). Their molecular weights as determined by affinity cross-linking with their respective 125I-ligands were similarly 70,000. The membrane-localized receptors could be solubilized with reduced Triton X-100 in the presence of 20% glycerol with good retention of hormone binding activity. The Triton extracts of membranes also showed hormone specificity and equilibrium binding constants similar to the membrane receptors (Kd = 32-48 pM). Affinity chromatography on divinylsulfonyl-Sepharose-oLH columns was utilized to purify the solubilized LH/hCG receptor to a specific activity of 2000 pmol/mg of protein. The purified receptor exhibited a high specificity for hCG and hLH but not for hFSH nor bTSH. The purified receptor was iodinated and visualized to be composed of a major protein of Mr approximately 70,000 and other minor proteins of molecular weights ranging from 14,000 to 40,000. Except for the Mr 14,000 protein, all other protein species bound to the concanavalin A-Sepharose column. The data suggest that the ovarian LH/hCG and FSH receptors are structurally similar and consist of a single polypeptide chain, as recently documented for the LH/hCG receptor (Loosefelt et al., 1989; McFarland et al., 1989).</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00467a022</identifier><identifier>PMID: 2340270</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>550601 - Medicine- Unsealed Radionuclides in Diagnostics ; ANIMAL CELLS ; ANIMALS ; AUTORADIOGRAPHY ; BETA DECAY RADIOISOTOPES ; binding ; Binding, Competitive ; Biological and medical sciences ; BODY ; CELL CONSTITUENTS ; Cell Membrane - analysis ; CELL MEMBRANES ; Cell receptors ; Cell structures and functions ; CHEMICAL REACTIONS ; Chromatography, Affinity ; CROSS-LINKING ; Cross-Linking Reagents - metabolism ; DAYS LIVING RADIOISOTOPES ; DOMESTIC ANIMALS ; ELECTRON CAPTURE RADIOISOTOPES ; Female ; FEMALE GENITALS ; follicle-stimulating hormone ; follicular fluid ; Follicular Fluid - analysis ; FSH ; Fundamental and applied biological sciences. Psychology ; GONADOTROPINS ; GONADS ; Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors ; hormone specificity ; HORMONES ; INTERMEDIATE MASS NUCLEI ; IODINE 125 ; IODINE ISOTOPES ; isolation ; ISOTOPES ; LH ; LIGANDS ; luteinizing hormone ; MAMMALS ; MEMBRANE PROTEINS ; MEMBRANES ; Molecular and cellular biology ; MOLECULAR STRUCTURE ; MOLECULAR WEIGHT ; NUCLEI ; ODD-EVEN NUCLEI ; ORGANIC COMPOUNDS ; ORGANS ; OVARIES ; PEPTIDE HORMONES ; PEPTIDES ; PITUITARY HORMONES ; plasma membranes ; POLYMERIZATION ; POLYPEPTIDES ; PROTEINS ; PURIFICATION ; RADIOISOTOPES ; RADIOLOGY AND NUCLEAR MEDICINE ; RECEPTORS ; Receptors, FSH - metabolism ; Receptors, Gonadotropin - metabolism ; Receptors, LH - analysis ; Solubility ; SWINE ; TUMOR CELLS ; VERTEBRATES</subject><ispartof>Biochemistry (Easton), 1990-04, Vol.29 (15), p.3751-3759</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a466t-2c8441eff89c191fe4fbd8b30fad64f89d287635f05370aa257cde18e4785f8d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00467a022$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00467a022$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,780,784,885,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19631403$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2340270$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/6323263$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Yarney, T. A</creatorcontrib><creatorcontrib>Sairam, M. R</creatorcontrib><creatorcontrib>Bhargavi, G. N</creatorcontrib><creatorcontrib>Mohapatra, S. K</creatorcontrib><title>Purification and characterization of lutropin receptor from membranes of pig follicular fluid</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Membranes derived from free floating granulosa cells in porcine ovarian follicular fluid were used as a starting material for structural characterization of both LH/hCG and FSH receptors. The receptors were highly hormone-specific and showed single classes of high-affinity binding sites (Kd = 19-74 pM). Their molecular weights as determined by affinity cross-linking with their respective 125I-ligands were similarly 70,000. The membrane-localized receptors could be solubilized with reduced Triton X-100 in the presence of 20% glycerol with good retention of hormone binding activity. The Triton extracts of membranes also showed hormone specificity and equilibrium binding constants similar to the membrane receptors (Kd = 32-48 pM). Affinity chromatography on divinylsulfonyl-Sepharose-oLH columns was utilized to purify the solubilized LH/hCG receptor to a specific activity of 2000 pmol/mg of protein. The purified receptor exhibited a high specificity for hCG and hLH but not for hFSH nor bTSH. The purified receptor was iodinated and visualized to be composed of a major protein of Mr approximately 70,000 and other minor proteins of molecular weights ranging from 14,000 to 40,000. Except for the Mr 14,000 protein, all other protein species bound to the concanavalin A-Sepharose column. The data suggest that the ovarian LH/hCG and FSH receptors are structurally similar and consist of a single polypeptide chain, as recently documented for the LH/hCG receptor (Loosefelt et al., 1989; McFarland et al., 1989).</description><subject>550601 - Medicine- Unsealed Radionuclides in Diagnostics</subject><subject>ANIMAL CELLS</subject><subject>ANIMALS</subject><subject>AUTORADIOGRAPHY</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>binding</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>BODY</subject><subject>CELL CONSTITUENTS</subject><subject>Cell Membrane - analysis</subject><subject>CELL MEMBRANES</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>CHEMICAL REACTIONS</subject><subject>Chromatography, Affinity</subject><subject>CROSS-LINKING</subject><subject>Cross-Linking Reagents - metabolism</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>DOMESTIC ANIMALS</subject><subject>ELECTRON CAPTURE RADIOISOTOPES</subject><subject>Female</subject><subject>FEMALE GENITALS</subject><subject>follicle-stimulating hormone</subject><subject>follicular fluid</subject><subject>Follicular Fluid - analysis</subject><subject>FSH</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GONADOTROPINS</subject><subject>GONADS</subject><subject>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</subject><subject>hormone specificity</subject><subject>HORMONES</subject><subject>INTERMEDIATE MASS NUCLEI</subject><subject>IODINE 125</subject><subject>IODINE ISOTOPES</subject><subject>isolation</subject><subject>ISOTOPES</subject><subject>LH</subject><subject>LIGANDS</subject><subject>luteinizing hormone</subject><subject>MAMMALS</subject><subject>MEMBRANE PROTEINS</subject><subject>MEMBRANES</subject><subject>Molecular and cellular biology</subject><subject>MOLECULAR STRUCTURE</subject><subject>MOLECULAR WEIGHT</subject><subject>NUCLEI</subject><subject>ODD-EVEN NUCLEI</subject><subject>ORGANIC COMPOUNDS</subject><subject>ORGANS</subject><subject>OVARIES</subject><subject>PEPTIDE HORMONES</subject><subject>PEPTIDES</subject><subject>PITUITARY HORMONES</subject><subject>plasma membranes</subject><subject>POLYMERIZATION</subject><subject>POLYPEPTIDES</subject><subject>PROTEINS</subject><subject>PURIFICATION</subject><subject>RADIOISOTOPES</subject><subject>RADIOLOGY AND NUCLEAR MEDICINE</subject><subject>RECEPTORS</subject><subject>Receptors, FSH - metabolism</subject><subject>Receptors, Gonadotropin - metabolism</subject><subject>Receptors, LH - analysis</subject><subject>Solubility</subject><subject>SWINE</subject><subject>TUMOR CELLS</subject><subject>VERTEBRATES</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9rFDEUB_AgSl1XT57FoaA9yOjLj0lmjrKoFSpu2Ra8SMhkkjZ1ZjImGdD-9WaZpfYgeArJ-_BNXh5CzzG8xUDwu9YBMC4UEPIArXBFoGRNUz1EKwDgJWk4PEZPYrzJWwaCHaEjQhkQASv0fTsHZ51WyfmxUGNX6GsVlE4muNvl0Nuin1PwkxuLYLSZkg-FDX4oBjO0QY0m7s3krgrr-97puVcZ9LPrnqJHVvXRPDusa3T58cPF5rQ8-_rp8-b9WakY56kkumYMG2vrRuMGW8Ns29UtBas6zvJpR2rBaWWhogKUIpXQncG1YaKubN3RNTpecn1MTkbtktHX2o-j0UlySijhNKPXC5qC_zmbmOTgojZ9nzvwc5SiEYIR9n-IK4F5DSTDNwvUwccYjJVTcIMKvyUGuR-NvDearF8cYud2MN2dPcwi118d6ipq1dv8s9rFv5ENp5jB_nnl4lxM5tddXYUfkgsqKnmx3cnzLzuyPd98k5vsXy7eKi_VVciZlzsCmO5vBZ5j1-hkEUpHeePnMOZh_bOHP9HeuwM</recordid><startdate>19900417</startdate><enddate>19900417</enddate><creator>Yarney, T. A</creator><creator>Sairam, M. R</creator><creator>Bhargavi, G. N</creator><creator>Mohapatra, S. K</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</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>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19900417</creationdate><title>Purification and characterization of lutropin receptor from membranes of pig follicular fluid</title><author>Yarney, T. A ; Sairam, M. R ; Bhargavi, G. N ; Mohapatra, S. K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a466t-2c8441eff89c191fe4fbd8b30fad64f89d287635f05370aa257cde18e4785f8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>550601 - Medicine- Unsealed Radionuclides in Diagnostics</topic><topic>ANIMAL CELLS</topic><topic>ANIMALS</topic><topic>AUTORADIOGRAPHY</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>binding</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>BODY</topic><topic>CELL CONSTITUENTS</topic><topic>Cell Membrane - analysis</topic><topic>CELL MEMBRANES</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>CHEMICAL REACTIONS</topic><topic>Chromatography, Affinity</topic><topic>CROSS-LINKING</topic><topic>Cross-Linking Reagents - metabolism</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>DOMESTIC ANIMALS</topic><topic>ELECTRON CAPTURE RADIOISOTOPES</topic><topic>Female</topic><topic>FEMALE GENITALS</topic><topic>follicle-stimulating hormone</topic><topic>follicular fluid</topic><topic>Follicular Fluid - analysis</topic><topic>FSH</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GONADOTROPINS</topic><topic>GONADS</topic><topic>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</topic><topic>hormone specificity</topic><topic>HORMONES</topic><topic>INTERMEDIATE MASS NUCLEI</topic><topic>IODINE 125</topic><topic>IODINE ISOTOPES</topic><topic>isolation</topic><topic>ISOTOPES</topic><topic>LH</topic><topic>LIGANDS</topic><topic>luteinizing hormone</topic><topic>MAMMALS</topic><topic>MEMBRANE PROTEINS</topic><topic>MEMBRANES</topic><topic>Molecular and cellular biology</topic><topic>MOLECULAR STRUCTURE</topic><topic>MOLECULAR WEIGHT</topic><topic>NUCLEI</topic><topic>ODD-EVEN NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANS</topic><topic>OVARIES</topic><topic>PEPTIDE HORMONES</topic><topic>PEPTIDES</topic><topic>PITUITARY HORMONES</topic><topic>plasma membranes</topic><topic>POLYMERIZATION</topic><topic>POLYPEPTIDES</topic><topic>PROTEINS</topic><topic>PURIFICATION</topic><topic>RADIOISOTOPES</topic><topic>RADIOLOGY AND NUCLEAR MEDICINE</topic><topic>RECEPTORS</topic><topic>Receptors, FSH - metabolism</topic><topic>Receptors, Gonadotropin - metabolism</topic><topic>Receptors, LH - analysis</topic><topic>Solubility</topic><topic>SWINE</topic><topic>TUMOR CELLS</topic><topic>VERTEBRATES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yarney, T. A</creatorcontrib><creatorcontrib>Sairam, M. R</creatorcontrib><creatorcontrib>Bhargavi, G. N</creatorcontrib><creatorcontrib>Mohapatra, S. K</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yarney, T. A</au><au>Sairam, M. R</au><au>Bhargavi, G. N</au><au>Mohapatra, S. K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of lutropin receptor from membranes of pig follicular fluid</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1990-04-17</date><risdate>1990</risdate><volume>29</volume><issue>15</issue><spage>3751</spage><epage>3759</epage><pages>3751-3759</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Membranes derived from free floating granulosa cells in porcine ovarian follicular fluid were used as a starting material for structural characterization of both LH/hCG and FSH receptors. The receptors were highly hormone-specific and showed single classes of high-affinity binding sites (Kd = 19-74 pM). Their molecular weights as determined by affinity cross-linking with their respective 125I-ligands were similarly 70,000. The membrane-localized receptors could be solubilized with reduced Triton X-100 in the presence of 20% glycerol with good retention of hormone binding activity. The Triton extracts of membranes also showed hormone specificity and equilibrium binding constants similar to the membrane receptors (Kd = 32-48 pM). Affinity chromatography on divinylsulfonyl-Sepharose-oLH columns was utilized to purify the solubilized LH/hCG receptor to a specific activity of 2000 pmol/mg of protein. The purified receptor exhibited a high specificity for hCG and hLH but not for hFSH nor bTSH. The purified receptor was iodinated and visualized to be composed of a major protein of Mr approximately 70,000 and other minor proteins of molecular weights ranging from 14,000 to 40,000. Except for the Mr 14,000 protein, all other protein species bound to the concanavalin A-Sepharose column. The data suggest that the ovarian LH/hCG and FSH receptors are structurally similar and consist of a single polypeptide chain, as recently documented for the LH/hCG receptor (Loosefelt et al., 1989; McFarland et al., 1989).</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>2340270</pmid><doi>10.1021/bi00467a022</doi><tpages>9</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 1990-04, Vol.29 (15), p.3751-3759 |
| issn | 0006-2960 1520-4995 |
| language | eng |
| recordid | cdi_osti_scitechconnect_6323263 |
| source | MEDLINE; American Chemical Society Journals |
| subjects | 550601 - Medicine- Unsealed Radionuclides in Diagnostics ANIMAL CELLS ANIMALS AUTORADIOGRAPHY BETA DECAY RADIOISOTOPES binding Binding, Competitive Biological and medical sciences BODY CELL CONSTITUENTS Cell Membrane - analysis CELL MEMBRANES Cell receptors Cell structures and functions CHEMICAL REACTIONS Chromatography, Affinity CROSS-LINKING Cross-Linking Reagents - metabolism DAYS LIVING RADIOISOTOPES DOMESTIC ANIMALS ELECTRON CAPTURE RADIOISOTOPES Female FEMALE GENITALS follicle-stimulating hormone follicular fluid Follicular Fluid - analysis FSH Fundamental and applied biological sciences. Psychology GONADOTROPINS GONADS Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors hormone specificity HORMONES INTERMEDIATE MASS NUCLEI IODINE 125 IODINE ISOTOPES isolation ISOTOPES LH LIGANDS luteinizing hormone MAMMALS MEMBRANE PROTEINS MEMBRANES Molecular and cellular biology MOLECULAR STRUCTURE MOLECULAR WEIGHT NUCLEI ODD-EVEN NUCLEI ORGANIC COMPOUNDS ORGANS OVARIES PEPTIDE HORMONES PEPTIDES PITUITARY HORMONES plasma membranes POLYMERIZATION POLYPEPTIDES PROTEINS PURIFICATION RADIOISOTOPES RADIOLOGY AND NUCLEAR MEDICINE RECEPTORS Receptors, FSH - metabolism Receptors, Gonadotropin - metabolism Receptors, LH - analysis Solubility SWINE TUMOR CELLS VERTEBRATES |
| title | Purification and characterization of lutropin receptor from membranes of pig follicular fluid |
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