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Titolo:
SYNTHESIS OF VITELLOGENIN POLYPEPTIDES AND DEPOSIT OF YOLK PROTEINS IN ANOLIS-PULCHELLUS
Autore:
MORALES MH; BAERGASANTINI C; CORDEROLOPEZ N;
Indirizzi:
UNIV PUERTO RICO,DEPT BIOL JGD107,POB 23360 SAN JUAN PR 00931
Titolo Testata:
Comparative biochemistry and physiology. B. Comparative biochemistry
fascicolo: 2, volume: 114, anno: 1996,
pagine: 225 - 231
SICI:
0305-0491(1996)114:2<225:SOVPAD>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRECURSOR-PRODUCT RELATIONSHIP; STIMULATED XENOPUS-LAEVIS; LACERTA-VIVIPARA JACQUIN; DENSITY-LIPOPROTEIN; PLASMA VITELLOGENIN; SALMO-GAIRDNERI; OVARIAN UPTAKE; RAINBOW-TROUT; LIVER; IDENTIFICATION;
Keywords:
ANOLINE LIZARD; LIPOPROTEIN; LIPOVITELLIN; PHOSPHOPROTEIN; PRECURSOR-PRODUCT RELATIONSHIP; REPTILIAN VITELLOGENESIS; VITELLOGENIN; YOLK PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
M.H. Morales et al., "SYNTHESIS OF VITELLOGENIN POLYPEPTIDES AND DEPOSIT OF YOLK PROTEINS IN ANOLIS-PULCHELLUS", Comparative biochemistry and physiology. B. Comparative biochemistry, 114(2), 1996, pp. 225-231

Abstract

The recognition of liver and serum polypeptides in Anolis pulchellus by a polyclonal antibody against S1-lipovitellin confirmed their identity as vitellogenins (Vtg) and demonstrated their structural relationship to yolk lipoproteins. In vivo labeling demonstrated active synthesis of Vtg by vitellogenic females since intracellular incorporation of[H-3]-leucine was detected at short periods of label in all five Anolis Vtg forms. Time course analysis of H-3-Vtg levels indicated a 1 hr lag phase between synthesis and secretion. On the other hand, P-32-Vtgappears to be rapidly secreted from the liver into the blood since label was detected simultaneously in both compartments. After 2 hr intracellular P-32-Vtg levels reached a plateau. Decreasing P-32-Vtg levelsin the blood were observed several hours after injection. In growing oocytes P-32 was detected in yolk phosphoproteins ranging from 37,000 to 75,000 in molecular weight. Based on these results together with previous published data we conclude that in tropical anole the yolk phosphoproteins appear to be derived from the Larger highly phosphorylatedVtg forms according to the typical vertebrate Vtg precursor-product relationship. However, the main component oi yolk lipovitellin is synthesized in the liver as an independent lipoprotein (Vtg-116) which is taken up by growing oocytes without major proteolytic modifications. This novel mode of lipovitellin biosynthesis and deposit in reptiles hasnot been reported previously.

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Documento generato il 10/07/20 alle ore 17:36:27