Lipovitellins and phosvitins of the fertilized eggs during embryo growth in the oviparous lizard Podarcis sicula
Identifieur interne : 000A76 ( Istex/Corpus ); précédent : 000A75; suivant : 000A77Lipovitellins and phosvitins of the fertilized eggs during embryo growth in the oviparous lizard Podarcis sicula
Auteurs : Maurizio Romano ; Patrizia Rosanova ; Chiara Anteo ; Ermelinda LimatolaSource :
- Molecular Reproduction and Development [ 1040-452X ] ; 2002-11.
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Abstract
In the lizard Podarcis sicula, the major vitellogenin (VTG)‐derived yolk proteins, lipovitellins and phosvitins, were extracted from the yolk globules of laid and fertilized eggs at different periods of incubation up to 44 days close to hatching. Embryonic development was almost over at this time. Yolk proteins were isolated by precipitation in saturated (NH4)2SO4, separated on SDS–PAGE and detected by Western blotting with homologous polyclonal anti/VTG antibody. Two lipovitellins of 110 and 116 kDa were always present in the yolk of laid eggs after 1, 10, 18, and 44 days from oviposition. Both these proteins were glycosylated and were recognized by the anti/VTG antibody; their N‐terminal sequences were analyzed. Four phosvitins were detected in freshly laid eggs, but their number decreased during incubation, and after 44 days only a single protein of ≅ 6.5 kDa was present. The results indicated that, in this lizard, during embryonic development, lipovitellins remain unchanged, whereas the phosphorylated components of yolk undergo continuous degradation. Mol. Reprod. Dev. 63: 341–348, 2002. © 2002 Wiley‐Liss, Inc.
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DOI: 10.1002/mrd.90018
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ISTEX:4F803E60EA21A29F87B93E36DED42422E7899F63Le document en format XML
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Embryonic development was almost over at this time. Yolk proteins were isolated by precipitation in saturated (NH4)2SO4, separated on SDS–PAGE and detected by Western blotting with homologous polyclonal anti/VTG antibody. Two lipovitellins of 110 and 116 kDa were always present in the yolk of laid eggs after 1, 10, 18, and 44 days from oviposition. Both these proteins were glycosylated and were recognized by the anti/VTG antibody; their N‐terminal sequences were analyzed. Four phosvitins were detected in freshly laid eggs, but their number decreased during incubation, and after 44 days only a single protein of ≅ 6.5 kDa was present. The results indicated that, in this lizard, during embryonic development, lipovitellins remain unchanged, whereas the phosphorylated components of yolk undergo continuous degradation. Mol. Reprod. 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Embryonic development was almost over at this time. Yolk proteins were isolated by precipitation in saturated (NH<sub>4</sub>)<sub>2</sub>SO<sub>4</sub>, separated on SDS–PAGE and detected by Western blotting with homologous polyclonal anti/VTG antibody. Two lipovitellins of 110 and 116 kDa were always present in the yolk of laid eggs after 1, 10, 18, and 44 days from oviposition. Both these proteins were glycosylated and were recognized by the anti/VTG antibody; their N‐terminal sequences were analyzed. Four phosvitins were detected in freshly laid eggs, but their number decreased during incubation, and after 44 days only a single protein of ≅ 6.5 kDa was present. The results indicated that, in this lizard, during embryonic development, lipovitellins remain unchanged, whereas the phosphorylated components of yolk undergo continuous degradation. Mol. Reprod. Dev. 63: 341–348, 2002. © 2002 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><p>This work is dedicated to Prof. Gianfranco Ghiara on the occasion of his 80th birthday.</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Lipovitellins and phosvitins of the fertilized eggs during embryo growth in the oviparous lizard Podarcis sicula</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>YOLK PROTEINS IN A LIZARD</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Lipovitellins and phosvitins of the fertilized eggs during embryo growth in the oviparous lizard Podarcis sicula</title></titleInfo><name type="personal"><namePart type="given">Maurizio</namePart><namePart type="family">Romano</namePart><affiliation>Department of Evolutionary and Comparative Biology, University Federico II, Via Mezzocannone, Napoli, Italy</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Patrizia</namePart><namePart type="family">Rosanova</namePart><affiliation>Department of Evolutionary and Comparative Biology, University Federico II, Via Mezzocannone, Napoli, Italy</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Chiara</namePart><namePart type="family">Anteo</namePart><affiliation>Department of Evolutionary and Comparative Biology, University Federico II, Via Mezzocannone, Napoli, Italy</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ermelinda</namePart><namePart type="family">Limatola</namePart><affiliation>Department of Evolutionary and Comparative Biology, University Federico II, Via Mezzocannone, Napoli, Italy</affiliation><affiliation>Department of Evolutionary and Comparative Biology, University of Napoli Federico II, Via Mezzocannone 8, 80134 Napoli, Italy.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2002-11</dateIssued><dateCaptured encoding="w3cdtf">2002-03-18</dateCaptured><dateValid encoding="w3cdtf">2002-05-29</dateValid><copyrightDate encoding="w3cdtf">2002</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">6</extent><extent unit="references">53</extent><extent unit="words">1391</extent></physicalDescription><abstract lang="en">In the lizard Podarcis sicula, the major vitellogenin (VTG)‐derived yolk proteins, lipovitellins and phosvitins, were extracted from the yolk globules of laid and fertilized eggs at different periods of incubation up to 44 days close to hatching. Embryonic development was almost over at this time. Yolk proteins were isolated by precipitation in saturated (NH4)2SO4, separated on SDS–PAGE and detected by Western blotting with homologous polyclonal anti/VTG antibody. Two lipovitellins of 110 and 116 kDa were always present in the yolk of laid eggs after 1, 10, 18, and 44 days from oviposition. Both these proteins were glycosylated and were recognized by the anti/VTG antibody; their N‐terminal sequences were analyzed. Four phosvitins were detected in freshly laid eggs, but their number decreased during incubation, and after 44 days only a single protein of ≅ 6.5 kDa was present. The results indicated that, in this lizard, during embryonic development, lipovitellins remain unchanged, whereas the phosphorylated components of yolk undergo continuous degradation. Mol. Reprod. Dev. 63: 341–348, 2002. © 2002 Wiley‐Liss, Inc.</abstract><note type="content">*This work is dedicated to Prof. Gianfranco Ghiara on the occasion of his 80th birthday.</note><note type="funding">Italian MIUR (Progetto Nazionale, Geremia group)</note><subject lang="en"><genre>keywords</genre><topic>reptiles</topic><topic>vitellogenesis</topic><topic>yolk proteins</topic><topic>embryonic development</topic><topic>albumen</topic></subject><relatedItem type="host"><titleInfo><title>Molecular Reproduction and Development</title><subTitle>Incorporating Gamete Research</subTitle></titleInfo><titleInfo type="abbreviated"><title>Mol. Reprod. Dev.</title></titleInfo><genre type="journal">journal</genre><subject><genre>article-category</genre><topic>Research Article</topic></subject><identifier type="ISSN">1040-452X</identifier><identifier type="eISSN">1098-2795</identifier><identifier type="DOI">10.1002/(ISSN)1098-2795</identifier><identifier type="PublisherID">MRD</identifier><part><date>2002</date><detail type="volume"><caption>vol.</caption><number>63</number></detail><detail type="issue"><caption>no.</caption><number>3</number></detail><extent unit="pages"><start>341</start><end>348</end><total>8</total></extent></part></relatedItem><identifier type="istex">4F803E60EA21A29F87B93E36DED42422E7899F63</identifier><identifier type="DOI">10.1002/mrd.90018</identifier><identifier type="ArticleID">MRD90018</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2002 Wiley‐Liss, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Wiley Subscription Services, Inc., A Wiley Company</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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