Isolation and characterization of insulin in Russian sturgeon (Acipenser guldenstaedti).
Identifieur interne : 000625 ( PubMed/Checkpoint ); précédent : 000624; suivant : 000626Isolation and characterization of insulin in Russian sturgeon (Acipenser guldenstaedti).
Auteurs : Rusakov YuI ; S. Moriyama ; V M Bondareva ; A P Kolychev ; Y. Amemiya ; A. Yasuda ; H. KawauchiSource :
- The journal of peptide research : official journal of the American Peptide Society [ 1397-002X ] ; 1998.
English descriptors
- KwdEn :
- MESH :
- chemical , isolation & purification : Insulin.
- metabolism : Cell Membrane, Fishes, Insulin, Receptor, Insulin.
- Amino Acid Sequence, Animals, Female, Humans, In Vitro Techniques, Male, Molecular Sequence Data, Radioimmunoassay, Rats.
Abstract
Insulin was isolated from the pancreas of Chondrostean fish, the Russian sturgeon, Acipenser guldenstaedti, by acid-ethanol extraction followed by ion-exchange and reverse-phase high-performance liquid chromatographies. The amino acid sequence determined by automated Edman degradation is as follows: A-chain (21-amino-acid peptide), H-Gly-Ile-Val-Glu-Gln-Cys-Cys-His-Ser-Pro-Cys-Ser-Leu-Tyr-Asp-Leu-Glu-As n-Tyr-Cys-Asn-OH; and B-chain (31-amino-acid peptide), H-Ala-Ala-Asn-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-Va l-Cys-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Asn-Lys-Val-OH. The sturgeon insulin appears to be identical with one of two forms of paddlefish insulin and differs from the other form by a single substitution in the A-chain, Asp15: His15. The amino acid sequence of sturgeon insulin is more similar to the amino acid sequence of mammalian insulins than of other fish insulins. Sturgeon insulin showed parallel but weaker displacement than porcine insulin and pink salmon insulin in their respective radioimmunoassays and was less potent than porcine insulin in displacing radiolabeled porcine insulin bound to partially purified rat liver plasma membranes.
PubMed: 9650713
Affiliations:
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Moriyama</name></author><author><name sortKey="Bondareva, V M" sort="Bondareva, V M" uniqKey="Bondareva V" first="V M" last="Bondareva">V M Bondareva</name></author><author><name sortKey="Kolychev, A P" sort="Kolychev, A P" uniqKey="Kolychev A" first="A P" last="Kolychev">A P Kolychev</name></author><author><name sortKey="Amemiya, Y" sort="Amemiya, Y" uniqKey="Amemiya Y" first="Y" last="Amemiya">Y. Amemiya</name></author><author><name sortKey="Yasuda, A" sort="Yasuda, A" uniqKey="Yasuda A" first="A" last="Yasuda">A. Yasuda</name></author><author><name sortKey="Kawauchi, H" sort="Kawauchi, H" uniqKey="Kawauchi H" first="H" last="Kawauchi">H. Kawauchi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1998">1998</date><idno type="RBID">pubmed:9650713</idno><idno type="pmid">9650713</idno><idno type="wicri:Area/PubMed/Corpus">000669</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000669</idno><idno type="wicri:Area/PubMed/Curation">000669</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000669</idno><idno type="wicri:Area/PubMed/Checkpoint">000669</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000669</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Isolation and characterization of insulin in Russian sturgeon (Acipenser guldenstaedti).</title><author><name sortKey="Rusakov Yui" sort="Rusakov Yui" uniqKey="Rusakov Yui" last="Rusakov Yui">Rusakov YuI</name><affiliation><nlm:affiliation>Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Science, St. Petersburg.</nlm:affiliation><wicri:noCountry code="subField">St</wicri:noCountry></affiliation></author><author><name sortKey="Moriyama, S" sort="Moriyama, S" uniqKey="Moriyama S" first="S" last="Moriyama">S. Moriyama</name></author><author><name sortKey="Bondareva, V M" sort="Bondareva, V M" uniqKey="Bondareva V" first="V M" last="Bondareva">V M Bondareva</name></author><author><name sortKey="Kolychev, A P" sort="Kolychev, A P" uniqKey="Kolychev A" first="A P" last="Kolychev">A P Kolychev</name></author><author><name sortKey="Amemiya, Y" sort="Amemiya, Y" uniqKey="Amemiya Y" first="Y" last="Amemiya">Y. Amemiya</name></author><author><name sortKey="Yasuda, A" sort="Yasuda, A" uniqKey="Yasuda A" first="A" last="Yasuda">A. Yasuda</name></author><author><name sortKey="Kawauchi, H" sort="Kawauchi, H" uniqKey="Kawauchi H" first="H" last="Kawauchi">H. Kawauchi</name></author></analytic><series><title level="j">The journal of peptide research : official journal of the American Peptide Society</title><idno type="ISSN">1397-002X</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Membrane (metabolism)</term><term>Female</term><term>Fishes (metabolism)</term><term>Humans</term><term>In Vitro Techniques</term><term>Insulin (isolation & purification)</term><term>Insulin (metabolism)</term><term>Male</term><term>Molecular Sequence Data</term><term>Radioimmunoassay</term><term>Rats</term><term>Receptor, Insulin (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Insulin</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Fishes</term><term>Insulin</term><term>Receptor, Insulin</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Female</term><term>Humans</term><term>In Vitro Techniques</term><term>Male</term><term>Molecular Sequence Data</term><term>Radioimmunoassay</term><term>Rats</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Insulin was isolated from the pancreas of Chondrostean fish, the Russian sturgeon, Acipenser guldenstaedti, by acid-ethanol extraction followed by ion-exchange and reverse-phase high-performance liquid chromatographies. The amino acid sequence determined by automated Edman degradation is as follows: A-chain (21-amino-acid peptide), H-Gly-Ile-Val-Glu-Gln-Cys-Cys-His-Ser-Pro-Cys-Ser-Leu-Tyr-Asp-Leu-Glu-As n-Tyr-Cys-Asn-OH; and B-chain (31-amino-acid peptide), H-Ala-Ala-Asn-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-Va l-Cys-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Asn-Lys-Val-OH. The sturgeon insulin appears to be identical with one of two forms of paddlefish insulin and differs from the other form by a single substitution in the A-chain, Asp15: His15. The amino acid sequence of sturgeon insulin is more similar to the amino acid sequence of mammalian insulins than of other fish insulins. Sturgeon insulin showed parallel but weaker displacement than porcine insulin and pink salmon insulin in their respective radioimmunoassays and was less potent than porcine insulin in displacing radiolabeled porcine insulin bound to partially purified rat liver plasma membranes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9650713</PMID><DateCreated><Year>1998</Year><Month>09</Month><Day>17</Day></DateCreated><DateCompleted><Year>1998</Year><Month>09</Month><Day>17</Day></DateCompleted><DateRevised><Year>2014</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1397-002X</ISSN><JournalIssue CitedMedium="Print"><Volume>51</Volume><Issue>6</Issue><PubDate><Year>1998</Year><Month>Jun</Month></PubDate></JournalIssue><Title>The journal of peptide research : official journal of the American Peptide Society</Title><ISOAbbreviation>J. Pept. Res.</ISOAbbreviation></Journal><ArticleTitle>Isolation and characterization of insulin in Russian sturgeon (Acipenser guldenstaedti).</ArticleTitle><Pagination><MedlinePgn>395-400</MedlinePgn></Pagination><Abstract><AbstractText>Insulin was isolated from the pancreas of Chondrostean fish, the Russian sturgeon, Acipenser guldenstaedti, by acid-ethanol extraction followed by ion-exchange and reverse-phase high-performance liquid chromatographies. The amino acid sequence determined by automated Edman degradation is as follows: A-chain (21-amino-acid peptide), H-Gly-Ile-Val-Glu-Gln-Cys-Cys-His-Ser-Pro-Cys-Ser-Leu-Tyr-Asp-Leu-Glu-As n-Tyr-Cys-Asn-OH; and B-chain (31-amino-acid peptide), H-Ala-Ala-Asn-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-Va l-Cys-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Asn-Lys-Val-OH. The sturgeon insulin appears to be identical with one of two forms of paddlefish insulin and differs from the other form by a single substitution in the A-chain, Asp15: His15. The amino acid sequence of sturgeon insulin is more similar to the amino acid sequence of mammalian insulins than of other fish insulins. Sturgeon insulin showed parallel but weaker displacement than porcine insulin and pink salmon insulin in their respective radioimmunoassays and was less potent than porcine insulin in displacing radiolabeled porcine insulin bound to partially purified rat liver plasma membranes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rusakov YuI</LastName><AffiliationInfo><Affiliation>Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Science, St. Petersburg.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Moriyama</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Bondareva</LastName><ForeName>V M</ForeName><Initials>VM</Initials></Author><Author ValidYN="Y"><LastName>Kolychev</LastName><ForeName>A P</ForeName><Initials>AP</Initials></Author><Author ValidYN="Y"><LastName>Amemiya</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Yasuda</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Kawauchi</LastName><ForeName>H</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Denmark</Country><MedlineTA>J Pept Res</MedlineTA><NlmUniqueID>9707067</NlmUniqueID><ISSNLinking>1397-002X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007328">Insulin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.10.1</RegistryNumber><NameOfSubstance UI="D011972">Receptor, Insulin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005399" MajorTopicYN="N">Fishes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D066298" MajorTopicYN="N">In Vitro Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007328" MajorTopicYN="N">Insulin</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011863" MajorTopicYN="N">Radioimmunoassay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011972" MajorTopicYN="N">Receptor, Insulin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1998</Year><Month>7</Month><Day>3</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1998</Year><Month>7</Month><Day>3</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1998</Year><Month>7</Month><Day>3</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9650713</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Amemiya, Y" sort="Amemiya, Y" uniqKey="Amemiya Y" first="Y" last="Amemiya">Y. Amemiya</name><name sortKey="Bondareva, V M" sort="Bondareva, V M" uniqKey="Bondareva V" first="V M" last="Bondareva">V M Bondareva</name><name sortKey="Kawauchi, H" sort="Kawauchi, H" uniqKey="Kawauchi H" first="H" last="Kawauchi">H. Kawauchi</name><name sortKey="Kolychev, A P" sort="Kolychev, A P" uniqKey="Kolychev A" first="A P" last="Kolychev">A P Kolychev</name><name sortKey="Moriyama, S" sort="Moriyama, S" uniqKey="Moriyama S" first="S" last="Moriyama">S. Moriyama</name><name sortKey="Rusakov Yui" sort="Rusakov Yui" uniqKey="Rusakov Yui" last="Rusakov Yui">Rusakov YuI</name><name sortKey="Yasuda, A" sort="Yasuda, A" uniqKey="Yasuda A" first="A" last="Yasuda">A. Yasuda</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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