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Titolo:
VITELLOGENIN IN TILAPIA (OREOCHROMIS-MOSSAMBICUS) - INDUCTION OF 2 FORMS BY ESTRADIOL, QUANTIFICATION IN PLASMA AND CHARACTERIZATION IN OOCYTE EXTRACT
Autore:
KISHIDA M; SPECKER JL;
Indirizzi:
UNIV RHODE ISL,DEPT ZOOL KINGSTON RI 02881
Titolo Testata:
Fish physiology and biochemistry
fascicolo: 3, volume: 12, anno: 1993,
pagine: 171 - 182
SICI:
0920-1742(1993)12:3<171:VIT(-I>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
TROUT SALMO-GAIRDNERI; EGG-YOLK PROTEINS; RAINBOW-TROUT; SERUM-PROTEIN; HOMOLOGOUS RADIOIMMUNOASSAY; CROSS-REACTIVITY; ORYZIAS-LATIPES; IDENTIFICATION; PURIFICATION; RECEPTOR;
Keywords:
TILAPIA (OREOCHROMIS-MOSSAMBICUS); VITELLOGENIN; ELISA; YOLK PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
M. Kishida e J.L. Specker, "VITELLOGENIN IN TILAPIA (OREOCHROMIS-MOSSAMBICUS) - INDUCTION OF 2 FORMS BY ESTRADIOL, QUANTIFICATION IN PLASMA AND CHARACTERIZATION IN OOCYTE EXTRACT", Fish physiology and biochemistry, 12(3), 1993, pp. 171-182

Abstract

Two forms of vitellogenin were isolated by DEAE agarose ion-exchange chromatography from plasma of the tilapia, Oreochromis mossambicus. The monomers have apparent molecular masses of 200 and 130 kDa, as indicated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), and a totalamount of phosphorus of 1.7 and 0.1%, respectively. Antibodies specific to the two forms, designated tVTG-200 and tVTG-130, were generated in rabbits and used to develop enzyme-linked immunosorbent assays (ELISAs) and in Western blot analyses of plasma and oocyte extract. SDS-PAGE of the oocyte extract showed a major protein band at 106.6, minor bands at 26.6, 24.2, and 23.7 kDa, and very faint bands at 83.4 and 17.5 kDa. Western blots of the oocyte extract revealed that the antiserumto tVTG-200 recognized strongly the protein bands at 24.2 and 23.7 kDa, and less strongly the bands at 25.1 and 22.6 kDa, whereas the antiserum to tVTG-130 recognized mainly the protein band at 106.6 kDa. The presence of both VTGs in untreated male tilapia was detected with the ELISAs using relatively high plasma volumes. Their presence in males was confirmed by VTG-like immunoreactive materials eluting from the ion-exchange column at the same positions as tVTG-200 and tVTG-130. The concentrations of the VTGs in males were several orders of magnitude lower than in vitellogenic females. Treatment of male tilapia with estradiol-17beta (E2) induced both VTGs within 24h. After 7 days, tVTG-130 reached a maximum concentration in plasma, whereas tVTG-200 continued to increase. Our findings demonstrate that the two vitellogenins are biochemically distinct, possibly differentially regulated, and made by both sexes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 04:38:47