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Titolo:
Partial characterization of vitellin and localization of vitellogenin production in the terrestrial isopod, Armadillidium vulgare
Autore:
Okuno, A; Katayama, H; Nagasawa, H;
Indirizzi:
Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo1138657, Japan Univ Tokyo Tokyo Japan 1138657 Biol Chem, Bunkyo Ku, Tokyo1138657, Japan
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
fascicolo: 3, volume: 126, anno: 2000,
pagine: 397 - 407
SICI:
0305-0491(200007)126:3<397:PCOVAL>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
MATURE FEMALE HEMOLYMPH; FRESH-WATER PRAWN; PENAEUS-MONODON; MACROBRACHIUM-ROSENBERGII; PROTEIN VITELLOGENIN; COMMON ANCESTRY; FAT-BODY; OVARY; SITE; CRUSTACEA;
Keywords:
vitellin; vitellogenin; isopod; Armadillidium vulgare; fat body; crustacea; ovary; woodlouse; egg;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Nagasawa, H Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo1138657, Japan Univ Tokyo Tokyo Japan 1138657 unkyo Ku, Tokyo1138657, Japan
Citazione:
A. Okuno et al., "Partial characterization of vitellin and localization of vitellogenin production in the terrestrial isopod, Armadillidium vulgare", COMP BIOC B, 126(3), 2000, pp. 397-407

Abstract

Vitellins were purified separately from ovaries and eggs of the isopod, Armadillidium vulgare. Ovarian vitellin consisted of at least six proteins with relative molecular masses of 205, 200, 185, 180, 122 and 112 kDa. The larger four proteins disappeared in eggs within a week after oviposition and a 59-kDa protein appeared thereafter. The amino-terminal amino acid sequences of these vitellin proteins were identical except for the ovarian 112 kDa, egg 112 kDa and 59 kDa proteins, and showed considerable similarity to those of known vitellogenins from other animals. Comparison of tryptic peptide maps of the 122 and 113 kDa proteins from eggs on reversed-phase HPLC andsequence identification of two randomly selected peaks having the same retention times indicated that two peptides were mostly similar in sequence. PCR-assisted cloning of the 5' region of a cDNA (591 bp) encoding vitellogenin revealed the presence of a signal peptide consisting of 16 amino acid residues and clarified the structural relationship among the protein components except for the ovarian 112 kDa and the egg 59 kDa proteins. Northern blot analysis revealed that the fat body is the main vitellogenin producing organ. (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 19/09/20 alle ore 08:09:49