Conformation of sturgeon pituitary somatotropin.
Identifieur interne : 000704 ( PubMed/Checkpoint ); précédent : 000703; suivant : 000705Conformation of sturgeon pituitary somatotropin.
Auteurs : T A Bewley ; H. PapkoffSource :
- International journal of peptide and protein research [ 0367-8377 ] ; 1987.
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Peptide Fragments.
- chemical : Growth Hormone, Thermolysin, Trypsin.
- Animals, Fishes, Protein Conformation, Spectrophotometry, Ultraviolet.
Abstract
Pituitary somatotropin (growth hormone) from the sturgeon (Acipenser gulden-stadti) has been studied by zero-order and second-order absorption spectroscopy, as well as by circular dichroism. Difference absorption spectra have also been generated during proteolytic digestion of the hormone. The molar extinction coefficient of the native protein was found to be 15,000 +/- 110 M-1 cm-1 at 278.5 nm. Comparison of the conformations of sturgeon somatotropin and somatotropins isolated from several mammalian species, including bovine and human, indicates a close relationship between these molecules. Such similarities may be related to the relatively high biopotency of this fish hormone in mammalian assay systems.
PubMed: 3610472
Affiliations:
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Papkoff</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1987">1987</date><idno type="RBID">pubmed:3610472</idno><idno type="pmid">3610472</idno><idno type="wicri:Area/PubMed/Corpus">000756</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000756</idno><idno type="wicri:Area/PubMed/Curation">000756</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000756</idno><idno type="wicri:Area/PubMed/Checkpoint">000756</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000756</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Conformation of sturgeon pituitary somatotropin.</title><author><name sortKey="Bewley, T A" sort="Bewley, T A" uniqKey="Bewley T" first="T A" last="Bewley">T A Bewley</name></author><author><name sortKey="Papkoff, H" sort="Papkoff, H" uniqKey="Papkoff H" first="H" last="Papkoff">H. Papkoff</name></author></analytic><series><title level="j">International journal of peptide and protein research</title><idno type="ISSN">0367-8377</idno><imprint><date when="1987" type="published">1987</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Fishes</term><term>Growth Hormone</term><term>Peptide Fragments (analysis)</term><term>Protein Conformation</term><term>Spectrophotometry, Ultraviolet</term><term>Thermolysin</term><term>Trypsin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Peptide Fragments</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Growth Hormone</term><term>Thermolysin</term><term>Trypsin</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Fishes</term><term>Protein Conformation</term><term>Spectrophotometry, Ultraviolet</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Pituitary somatotropin (growth hormone) from the sturgeon (Acipenser gulden-stadti) has been studied by zero-order and second-order absorption spectroscopy, as well as by circular dichroism. Difference absorption spectra have also been generated during proteolytic digestion of the hormone. The molar extinction coefficient of the native protein was found to be 15,000 +/- 110 M-1 cm-1 at 278.5 nm. Comparison of the conformations of sturgeon somatotropin and somatotropins isolated from several mammalian species, including bovine and human, indicates a close relationship between these molecules. Such similarities may be related to the relatively high biopotency of this fish hormone in mammalian assay systems.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">3610472</PMID><DateCreated><Year>1987</Year><Month>09</Month><Day>21</Day></DateCreated><DateCompleted><Year>1987</Year><Month>09</Month><Day>21</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0367-8377</ISSN><JournalIssue CitedMedium="Print"><Volume>29</Volume><Issue>5</Issue><PubDate><Year>1987</Year><Month>May</Month></PubDate></JournalIssue><Title>International journal of peptide and protein research</Title><ISOAbbreviation>Int. J. Pept. Protein Res.</ISOAbbreviation></Journal><ArticleTitle>Conformation of sturgeon pituitary somatotropin.</ArticleTitle><Pagination><MedlinePgn>568-73</MedlinePgn></Pagination><Abstract><AbstractText>Pituitary somatotropin (growth hormone) from the sturgeon (Acipenser gulden-stadti) has been studied by zero-order and second-order absorption spectroscopy, as well as by circular dichroism. Difference absorption spectra have also been generated during proteolytic digestion of the hormone. The molar extinction coefficient of the native protein was found to be 15,000 +/- 110 M-1 cm-1 at 278.5 nm. Comparison of the conformations of sturgeon somatotropin and somatotropins isolated from several mammalian species, including bovine and human, indicates a close relationship between these molecules. Such similarities may be related to the relatively high biopotency of this fish hormone in mammalian assay systems.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bewley</LastName><ForeName>T A</ForeName><Initials>TA</Initials></Author><Author ValidYN="Y"><LastName>Papkoff</LastName><ForeName>H</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>AM-18677</GrantID><Acronym>AM</Acronym><Agency>NIADDK NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AM-6097</GrantID><Acronym>AM</Acronym><Agency>NIADDK NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Denmark</Country><MedlineTA>Int J Pept Protein Res</MedlineTA><NlmUniqueID>0330420</NlmUniqueID><ISSNLinking>0367-8377</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>9002-72-6</RegistryNumber><NameOfSubstance UI="D013006">Growth Hormone</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance UI="D014357">Trypsin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.27</RegistryNumber><NameOfSubstance UI="D013820">Thermolysin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005399" MajorTopicYN="N">Fishes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013006" MajorTopicYN="Y">Growth Hormone</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013056" MajorTopicYN="N">Spectrophotometry, Ultraviolet</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013820" MajorTopicYN="N">Thermolysin</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014357" MajorTopicYN="N">Trypsin</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1987</Year><Month>5</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1987</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1987</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">3610472</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Bewley, T A" sort="Bewley, T A" uniqKey="Bewley T" first="T A" last="Bewley">T A Bewley</name><name sortKey="Papkoff, H" sort="Papkoff, H" uniqKey="Papkoff H" first="H" last="Papkoff">H. 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