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Titolo:
PURIFICATION AND CHARACTERIZATION OF VITELLIN FROM THE MATURE OVARIESOF PRAWN, PENAEUS-CHINENSIS
Autore:
CHANG CF; JENG SR; LIN MN; TIN YY;
Indirizzi:
NATL TAIWAN OCEAN UNIV,DEPT AQUACULTURE CHILUNG 20224 TAIWAN NATL KAOSHIUNG JUNIOR COLL MARINE TECHNOL,DEPT AQUACULTURE KAOHSIUNG 81105 TAIWAN TAIWAN FISHERIES RES INST TAINAN 72401 TAIWAN
Titolo Testata:
INVERTEBRATE REPRODUCTION & DEVELOPMENT
fascicolo: 2, volume: 29, anno: 1996,
pagine: 87 - 93
SICI:
0792-4259(1996)29:2<87:PACOVF>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PARAPENAEUS-LONGIROSTRIS CRUSTACEA; PROTEIN VITELLOGENIN; FEMALE HEMOLYMPH; SHRIMP; LIPOVITELLIN; YOLK; IDENTIFICATION; LOCALIZATION; PENAEIDAE; JAPONICUS;
Keywords:
OVARY; PRAWN; VITELLIN; VITELLOGENIN; PENAEUS CHINENSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
C.F. Chang et al., "PURIFICATION AND CHARACTERIZATION OF VITELLIN FROM THE MATURE OVARIESOF PRAWN, PENAEUS-CHINENSIS", INVERTEBRATE REPRODUCTION & DEVELOPMENT, 29(2), 1996, pp. 87-93

Abstract

Purification and the characterization of ovarian vitellin of mature female prawn, Penaeus chinensis, were the objectives of this study. Mature ovaries were homogenized and purified with gel filtration, hydroxylapatite, polyacrylamide gel electrophoresis (PAGE) and electro-elution. Two forms of purified vitellin (Vn1,Vn2) were obtained with an apparent molecular weight of 380 kDa (Vn1) and 500 kDa (Vn2). These proteins reacted with antiserum raised against P. monodon vitellin, and theyhad a complete identity of an immunoprecipitation line when compared to the hemolymph vitellogenin of P. chinensis. Five subunits of Vn1 (105, 85, 78, 58 and 40 kDa) and three subunits of Vn2 (155, 85, 78 kDa)were detected with SDS-PAGE, Vn1 and Vn2 stained as a lipo-glyco-caroteno-phospho-protein and a glycophospho-protein, respectively. Vn1 wasmore abundant than Vn2. The amino acid composition of the purified Vn1 was determined. Difference in the number of polypeptide subunits - but a similarity in the amino acid composition - was observed between purified P. chinensis vitellogenin and vitellin. The biochemical characteristics might suggest that vitellogenin in hemolymph is incorporatedinto oocytes and then dissociated into two subunits (191 kDa and 85 kDa). One of the subunits (191 kDa) is partially digested and transformed into vitellin in combination with another subunit (85 kDa).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 09:42:28