Isolation and characterization of insulin in Russian sturgeon (Acipenser guldenstaedti).
Identifieur interne : 001744 ( Main/Curation ); précédent : 001743; suivant : 001745Isolation 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
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Rusakov YuI<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>Le document en format XML
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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. 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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></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></record>Pour manipuler ce document sous Unix (Dilib)
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