Neurohypophysal hormones as molecular evolutionary tracers : investigations on the surgeons Acipenser stellatus and Acipenser guldenstadti
Identifieur interne : 001D22 ( Main/Curation ); précédent : 001D21; suivant : 001D23Neurohypophysal hormones as molecular evolutionary tracers : investigations on the surgeons Acipenser stellatus and Acipenser guldenstadti
Auteurs : Y. Rouille [France] ; J. Chauvet ; M. T. Chauvet ; R. Acher ; A. L. PolenovSource :
- Comparative biochemistry and physiology. B. Comparative biochemistry [ 0305-0491 ] ; 1991.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
Abstract
1. Neurohypophysial hormones of two sturgeon species, Acipenser stellatus and Acipenser guldenstadti, have been purified through molecular sieving on Bio-Gel P4 and reverse-phase high pressure liquid chromatography on Nucleosil C18 columns. 2. Arginine vasotocin has been identified in both species by its retention time in partition chromatography, amino acid composition and, in the case of A. stellatus, by amino acid sequencing. 3. A second peptide has been purified and could be α-deamidated vasotocin
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Pascal:92-0470569Le document en format XML
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<author><name sortKey="Rouille, Y" sort="Rouille, Y" uniqKey="Rouille Y" first="Y." last="Rouille">Y. Rouille</name>
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<sZ>1 aut., 2 aut., 3 aut., 4 aut.</sZ>
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<country>France</country>
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<author><name sortKey="Chauvet, J" sort="Chauvet, J" uniqKey="Chauvet J" first="J." last="Chauvet">J. Chauvet</name>
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<author><name sortKey="Acher, R" sort="Acher, R" uniqKey="Acher R" first="R." last="Acher">R. Acher</name>
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<term>Vasopressin</term>
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<keywords scheme="Pascal" xml:lang="fr"><term>Analogue</term>
<term>Acipenser stellatus</term>
<term>Neurohypophyse</term>
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<front><div type="abstract" xml:lang="en">1. Neurohypophysial hormones of two sturgeon species, Acipenser stellatus and Acipenser guldenstadti, have been purified through molecular sieving on Bio-Gel P4 and reverse-phase high pressure liquid chromatography on Nucleosil C18 columns. 2. Arginine vasotocin has been identified in both species by its retention time in partition chromatography, amino acid composition and, in the case of A. stellatus, by amino acid sequencing. 3. A second peptide has been purified and could be α-deamidated vasotocin</div>
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