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Titolo:
Synthesis and organization of vitellogenin and vitellin molecules from theland crab Potamon potamios
Autore:
Pateraki, LE; Stratakis, E;
Indirizzi:
Univ Crete, Dept Biol, Heraklion, Crete, Greece Univ Crete Heraklion Crete Greece e, Dept Biol, Heraklion, Crete, Greece
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
fascicolo: 1, volume: 125, anno: 2000,
pagine: 53 - 61
SICI:
0305-0491(200001)125:1<53:SAOOVA>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
MATURE FEMALE HEMOLYMPH; UCA-PUGILATOR; PROTEIN VITELLOGENIN; FIDDLER CRAB; CRUSTACEA; OVARY; PRAWN; PURIFICATION; LIPOVITELLIN; LIPOPROTEIN;
Keywords:
brachyura crustacea; molecular organization; vitellogenin; vitellin; eyestalk ablated female;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Stratakis, E Univ Crete, Dept Biol, POB 714 09, Heraklion, Crete, Greece Univ Crete POB 714 09 Heraklion Crete Greece , Crete, Greece
Citazione:
L.E. Pateraki e E. Stratakis, "Synthesis and organization of vitellogenin and vitellin molecules from theland crab Potamon potamios", COMP BIOC B, 125(1), 2000, pp. 53-61

Abstract

We have previously reported that vitellogenin (Vg) of some female animals contained four polypeptides with molecular mass of 181, 115, 105 and 85 kDa, whereas Vg of most animals contained three polypeptides with molecular mass of 115, 105 and 85 kDa. In the present investigation, we examined whether the 181 kDa polypeptide is the precursor of 115 and 105 kDa Vg and vitellin (Vn) polypeptides. Labeling studies, using [S-35]methionine on normal vitellogenic animals, showed that the radioactivity was distributed first among the 181 and 85 kDa polypeptides. SDS-PAGE analysis of purified hemolymphVg from eyestalk ablated female animals revealed in most animals two polypeptides with an apparent molecular mass of 181 and 85 kDa. These results from in vivo experiments corroborated the view that the 115 and 105 kDa Vg and Vn polypeptides are derived from heaviest 181 kDa polypeptide. In addition it was demonstrated that hepatopancreas and ovary of Potamon potamios incubated in vitro with [S-35]methionine synthesized five polypeptides with apparent molecular mass of 224, 181, 115, 105, and 85 kDa while the hepatopancreas appeared to secrete the 181, 115, 105 and 85 kDa polypeptides. The major 115, 105 and 85 kDa polypeptides were found to be components of egg Vn,while the 224 kDa polypeptide was found to be minor component of Vg and Vnfrom hepatopancreas and ovary extracts, respectively. We conclude that theVn polypeptides produced by ovary are similar to those produced by hepatopancreas. (C) 2000 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/08/20 alle ore 00:55:29