Isolation and Amino Acid Sequence of Corticotropin-Releasing Factor from Pig Hypothalami
A polypeptide was isolated from acid extracts of porcine hypothalami on the basis of its high ability to stimulate the release of corticotropin from superfused rat pituitary cells. After an initial separation by gel filtration on Sephadex G-25, further purification was carried out by reversed-phase...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1985-12, Vol.82 (24), p.8762-8766 |
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creator | Patthy, Miklos Horvath, Judit Mason-Garcia, Meredith Szoke, Balazs Schlesinger, David H. Schally, Andrew V. |
description | A polypeptide was isolated from acid extracts of porcine hypothalami on the basis of its high ability to stimulate the release of corticotropin from superfused rat pituitary cells. After an initial separation by gel filtration on Sephadex G-25, further purification was carried out by reversed-phase HPLC. The isolated material was homogeneous chromatographically and by N-terminal sequencing. Based on automated gas-phase sequencing of the intact and CNBr-cleaved peptide and on carboxypeptidase Y digestion, the primary structure of this 41-residue polypeptide was determined to be Ser-Glu-Glu-Pro-Pro-Ile-Ser-Leu_Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-Met-Ala-Arg-Ala-Glu-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn-Arg-Lys-Leu-Met-Glu-Asn-Phe-NH2. Porcine corticotropin-releasing factor (CRF) shares a common amino acid sequence (residues 1-39) with rat and human CRF and differs from these only in positions 40 and 41. However, isoleucine was also present at position 40 in porcine CRF, but in a smaller percentage than asparagine. The sequence of porcine CRF shows 83% homology with ovine CRF. Porcine CRF markedly stimulated the release of corticotropin from superfused rat and pig pituitary cells. The biological activity and close structural relationship to CRFs of other species indicate that the peptide isolated represents porcine CRF. |
doi_str_mv | 10.1073/pnas.82.24.8762 |
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After an initial separation by gel filtration on Sephadex G-25, further purification was carried out by reversed-phase HPLC. The isolated material was homogeneous chromatographically and by N-terminal sequencing. Based on automated gas-phase sequencing of the intact and CNBr-cleaved peptide and on carboxypeptidase Y digestion, the primary structure of this 41-residue polypeptide was determined to be Ser-Glu-Glu-Pro-Pro-Ile-Ser-Leu_Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-Met-Ala-Arg-Ala-Glu-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn-Arg-Lys-Leu-Met-Glu-Asn-Phe-NH2. Porcine corticotropin-releasing factor (CRF) shares a common amino acid sequence (residues 1-39) with rat and human CRF and differs from these only in positions 40 and 41. However, isoleucine was also present at position 40 in porcine CRF, but in a smaller percentage than asparagine. The sequence of porcine CRF shows 83% homology with ovine CRF. Porcine CRF markedly stimulated the release of corticotropin from superfused rat and pig pituitary cells. The biological activity and close structural relationship to CRFs of other species indicate that the peptide isolated represents porcine CRF.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.82.24.8762</identifier><identifier>PMID: 3878520</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Amino acids ; Aminoacids, peptides. Hormones. Neuropeptides ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Chromatography, High Pressure Liquid ; Corticotropin-Releasing Hormone - isolation & purification ; Elution ; Endocrinology ; Fundamental and applied biological sciences. Psychology ; Hormones ; Hypothalamus - analysis ; Medical sciences ; Proteins ; Rats ; Sequencing ; Sheep ; Solvents ; Swine</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1985-12, Vol.82 (24), p.8762-8766</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c556t-9c5dfc25e9e2f6c62d2df39874386179da730ce7ad1d1ce90c4f1a516630ecc73</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/82/24.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/26672$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/26672$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,729,782,786,805,887,27931,27932,53798,53800,58024,58257</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8637331$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3878520$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Patthy, Miklos</creatorcontrib><creatorcontrib>Horvath, Judit</creatorcontrib><creatorcontrib>Mason-Garcia, Meredith</creatorcontrib><creatorcontrib>Szoke, Balazs</creatorcontrib><creatorcontrib>Schlesinger, David H.</creatorcontrib><creatorcontrib>Schally, Andrew V.</creatorcontrib><title>Isolation and Amino Acid Sequence of Corticotropin-Releasing Factor from Pig Hypothalami</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>A polypeptide was isolated from acid extracts of porcine hypothalami on the basis of its high ability to stimulate the release of corticotropin from superfused rat pituitary cells. After an initial separation by gel filtration on Sephadex G-25, further purification was carried out by reversed-phase HPLC. The isolated material was homogeneous chromatographically and by N-terminal sequencing. Based on automated gas-phase sequencing of the intact and CNBr-cleaved peptide and on carboxypeptidase Y digestion, the primary structure of this 41-residue polypeptide was determined to be Ser-Glu-Glu-Pro-Pro-Ile-Ser-Leu_Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-Met-Ala-Arg-Ala-Glu-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn-Arg-Lys-Leu-Met-Glu-Asn-Phe-NH2. Porcine corticotropin-releasing factor (CRF) shares a common amino acid sequence (residues 1-39) with rat and human CRF and differs from these only in positions 40 and 41. However, isoleucine was also present at position 40 in porcine CRF, but in a smaller percentage than asparagine. The sequence of porcine CRF shows 83% homology with ovine CRF. Porcine CRF markedly stimulated the release of corticotropin from superfused rat and pig pituitary cells. The biological activity and close structural relationship to CRFs of other species indicate that the peptide isolated represents porcine CRF.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Aminoacids, peptides. Hormones. Neuropeptides</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Corticotropin-Releasing Hormone - isolation & purification</subject><subject>Elution</subject><subject>Endocrinology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormones</subject><subject>Hypothalamus - analysis</subject><subject>Medical sciences</subject><subject>Proteins</subject><subject>Rats</subject><subject>Sequencing</subject><subject>Sheep</subject><subject>Solvents</subject><subject>Swine</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUuLFDEUhYMoYzu6FgQlC9FV9eRRedTCRdM4zsCA4gPchZhKejKkkjJJi_PvraKLQjeu7uJ8574OAM8x2mIk6MUYddlKsiXtVgpOHoANRh1ueNuhh2CDEBGNbEn7GDwp5Q4h1DGJzsAZlUIygjbg-3VJQVefItSxh7vBxwR3xvfwi_15tNFYmBzcp1y9STWn0cfmsw1WFx8P8FKbmjJ0OQ3wkz_Aq_sx1Vsd9OCfgkdOh2KfLfUcfLt8_3V_1dx8_HC93900hjFem86w3hnCbGeJ44aTnvSOdlK0VHIsul4LiowVusc9NrZDpnVYM8w5RdYYQc_Bu1Pf8fhjsL2xsWYd1Jj9oPO9Stqrf5Xob9Uh_VK0wwzP_jeLP6fp4FLV4IuxIeho07EowVlLCGYTeHECTU6lZOvWGRipOQs1Z6EkUaRVcxaT4-Xfq6388vxJf73ouhgdXNbR-LJiklNBKZ6wtws291_VdY5yxxCq_V0n8tV_yQl4cQLuypTbShDOBaF_AI8ftPg</recordid><startdate>19851201</startdate><enddate>19851201</enddate><creator>Patthy, Miklos</creator><creator>Horvath, Judit</creator><creator>Mason-Garcia, Meredith</creator><creator>Szoke, Balazs</creator><creator>Schlesinger, David H.</creator><creator>Schally, Andrew V.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19851201</creationdate><title>Isolation and Amino Acid Sequence of Corticotropin-Releasing Factor from Pig Hypothalami</title><author>Patthy, Miklos ; Horvath, Judit ; Mason-Garcia, Meredith ; Szoke, Balazs ; Schlesinger, David H. ; Schally, Andrew V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c556t-9c5dfc25e9e2f6c62d2df39874386179da730ce7ad1d1ce90c4f1a516630ecc73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Aminoacids, peptides. Hormones. Neuropeptides</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Corticotropin-Releasing Hormone - isolation & purification</topic><topic>Elution</topic><topic>Endocrinology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormones</topic><topic>Hypothalamus - analysis</topic><topic>Medical sciences</topic><topic>Proteins</topic><topic>Rats</topic><topic>Sequencing</topic><topic>Sheep</topic><topic>Solvents</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Patthy, Miklos</creatorcontrib><creatorcontrib>Horvath, Judit</creatorcontrib><creatorcontrib>Mason-Garcia, Meredith</creatorcontrib><creatorcontrib>Szoke, Balazs</creatorcontrib><creatorcontrib>Schlesinger, David H.</creatorcontrib><creatorcontrib>Schally, Andrew V.</creatorcontrib><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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Patthy, Miklos</au><au>Horvath, Judit</au><au>Mason-Garcia, Meredith</au><au>Szoke, Balazs</au><au>Schlesinger, David H.</au><au>Schally, Andrew V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and Amino Acid Sequence of Corticotropin-Releasing Factor from Pig Hypothalami</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1985-12-01</date><risdate>1985</risdate><volume>82</volume><issue>24</issue><spage>8762</spage><epage>8766</epage><pages>8762-8766</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>A polypeptide was isolated from acid extracts of porcine hypothalami on the basis of its high ability to stimulate the release of corticotropin from superfused rat pituitary cells. After an initial separation by gel filtration on Sephadex G-25, further purification was carried out by reversed-phase HPLC. The isolated material was homogeneous chromatographically and by N-terminal sequencing. Based on automated gas-phase sequencing of the intact and CNBr-cleaved peptide and on carboxypeptidase Y digestion, the primary structure of this 41-residue polypeptide was determined to be Ser-Glu-Glu-Pro-Pro-Ile-Ser-Leu_Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-Met-Ala-Arg-Ala-Glu-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn-Arg-Lys-Leu-Met-Glu-Asn-Phe-NH2. Porcine corticotropin-releasing factor (CRF) shares a common amino acid sequence (residues 1-39) with rat and human CRF and differs from these only in positions 40 and 41. However, isoleucine was also present at position 40 in porcine CRF, but in a smaller percentage than asparagine. The sequence of porcine CRF shows 83% homology with ovine CRF. Porcine CRF markedly stimulated the release of corticotropin from superfused rat and pig pituitary cells. The biological activity and close structural relationship to CRFs of other species indicate that the peptide isolated represents porcine CRF.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3878520</pmid><doi>10.1073/pnas.82.24.8762</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Amino acids Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Chromatography, High Pressure Liquid Corticotropin-Releasing Hormone - isolation & purification Elution Endocrinology Fundamental and applied biological sciences. Psychology Hormones Hypothalamus - analysis Medical sciences Proteins Rats Sequencing Sheep Solvents Swine |
title | Isolation and Amino Acid Sequence of Corticotropin-Releasing Factor from Pig Hypothalami |
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