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
Hauptverfasser: Patthy, Miklos, Horvath, Judit, Mason-Garcia, Meredith, Szoke, Balazs, Schlesinger, David H., Schally, Andrew V.
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container_end_page 8766
container_issue 24
container_start_page 8762
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 82
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. 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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><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 &amp; 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 &amp; 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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