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Titolo:
IDENTIFICATION OF 4 OVARIAN RECEPTOR PROTEINS THAT BIND VITELLOGENIN BUT NOT OTHER HOMOLOGOUS PLASMA-LIPOPROTEINS IN THE RAINBOW-TROUT, ONCORHYNCHUS-MYKISS
Autore:
TYLER CR; LUBBERINK K;
Indirizzi:
BRUNEL UNIV,DEPT BIOL & BIOCHEM UXBRIDGE UB8 3PH MIDDX ENGLAND
Titolo Testata:
Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology
fascicolo: 1, volume: 166, anno: 1996,
pagine: 11 - 20
SICI:
0174-1578(1996)166:1<11:IO4ORP>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
HIGH-DENSITY-LIPOPROTEIN; SALMO-GAIRDNERI; CHICKEN OOCYTE; PURIFICATION; MEMBRANES; FOLLICLES; SOLUBILIZATION; GLYCOPROTEINS; ASSOCIATION; LIVER;
Keywords:
VITELLOGENIN; LIPOPROTEINS; RECEPTOR; FOLLICLE; RAINBOW TROUT, ONCORHYNCHUS MYKISS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
C.R. Tyler e K. Lubberink, "IDENTIFICATION OF 4 OVARIAN RECEPTOR PROTEINS THAT BIND VITELLOGENIN BUT NOT OTHER HOMOLOGOUS PLASMA-LIPOPROTEINS IN THE RAINBOW-TROUT, ONCORHYNCHUS-MYKISS", Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology, 166(1), 1996, pp. 11-20

Abstract

Membrane proteins from ovarian follicles, testis and somatic tissues of rainbow trout, Oncorhynchus mykiss, were extracted by ultracentrifugation, separated on sodium dodecyl sulphate gels and isolated on polyvinyl difluoride membranes. Vitellogenin receptor proteins were visualised using protein staining and hybridisation with I-125-vitellogenin. Four follicle-membrane proteins, with molecular masses of 220, 210, 110 and 100 kDa, showed a strong affinity for vitellogenin and were specific to the ovary. Other homologous lipoproteins (very low density lipoprotein, low density lipoprotein and high density lipoprotein) had avery limited ability to displace I-125-vitellogenin from its receptor, indicating that the ovarian receptor proteins were fairly specific for vitellogenin. Proteins with an affinity for very low density lipoprotein and low density lipoprotein were visualised in liver, spleen andmuscle, eluting on sodium dodecyl sulphate gels with molecular massesof about 150 kDa. Peptides generated fi om trypsin digests of the receptor proteins with a high affinity for vitellogenin showed sequence homology with receptors in the lipoprotein family, including a sequencethat is believed to act as the internalisation signal [Phe-Asp-Asn-Phe-Tyr-] and a sequence identity with the recently characterised chicken vitellogenin/very low density lipoprotein receptor [Ser-Glu-Leu-Tyr-Glu-Pro-Ala-]. Together, the ligand blotting and peptide sequence datasupport the contention that the four ovarian membrane proteins isolated are receptor proteins specific for vitellogenin and they do not bind other plasma lipoproteins to any significant degree.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 11:24:46