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Titolo:
LIPOVITELLIN-2-BETA IS THE 31-KD NI2-BINDING PROTEIN (PNIXB) IN XENOPUS-OOCYTES AND EMBRYOS()
Autore:
GRBACIVANKOVIC S; ANTONIJCZUK K; VARGHESE AH; PLOWMAN MC; ANTONIJCZUK A; KORZA G; OZOLS J; SUNDERMAN FW;
Indirizzi:
UNIV CONNECTICUT,CTR HLTH,SCH MED,DEPT LAB MED,263 FARMINGTON AVE FARMINGTON CT 06030 UNIV CONNECTICUT,CTR HLTH,SCH MED,DEPT LAB MED FARMINGTON CT 06030 UNIV CONNECTICUT,SCH MED,DEPT BIOCHEM FARMINGTON CT 00000 UNIV CONNECTICUT,SCH MED,DEPT PHARMACOL FARMINGTON CT 06032
Titolo Testata:
Molecular reproduction and development
fascicolo: 3, volume: 38, anno: 1994,
pagine: 256 - 263
SICI:
1040-452X(1994)38:3<256:LIT3NP>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
NICKEL CHLORIDE; FETAX PROCEDURE; YOLK PROTEINS; LAEVIS; VITELLOGENIN; BINDING; TERATOGENICITY; MALFORMATIONS; EXPRESSION; OOGENESIS;
Keywords:
EMBRYOGENESIS; LIPOVITELLIN; METAL-BINDING PROTEINS; NICKEL TERATOGENESIS; TRACE METALS; YOLK PROTEINS; XENOPUS LAEVIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
S. Grbacivankovic et al., "LIPOVITELLIN-2-BETA IS THE 31-KD NI2-BINDING PROTEIN (PNIXB) IN XENOPUS-OOCYTES AND EMBRYOS()", Molecular reproduction and development, 38(3), 1994, pp. 256-263

Abstract

An Ni2+-binding protein (pNiXb, 31 kD) present in mature Xenopus laevis oocytes and in embryos from fertilization in N/F stage 42, was isolated and characterized. After oocytes or embryos were fractionated by PAGE, electroblotted onto nitrocellulose, and probed with Ni-63(2+), pNiXb was detected by autoradiography. pNiXb, a yolk protein located inthe embryonic gut, was purified from yolk platelets by ammonium sulfate precipitation, delipidation, gel filtration chromatography, and HPLC analysis. During these steps, pNiXb copurified with lipovitellin 2. The N-terminal sequence of purified pNiXb exactly matched that of Xenopus lipovitellin 2 beta, deduced from the DNA sequence of the Xenopus vitellogenin A2 precursor gene. Since pNiXb and lipovitellin 2 beta agree in N-terminal sequence, amino acid composition, and apparent molecular weight, they appear to be identical. Based on a metal-blot competition assay, the abilities of metal ions to compete with Ni-63(2+) forbinding to pNiXb were ranked: Zn2+ approximate to CU2+ approximate toCo2+ > Cd2+ approximate to Mn2+ > Sn2+. This study shows that Xenopuslipovitellin 2 beta is a metal-binding protein in vitro, and raises the possibility that it may function similarly in vivo. (C) 1994 Wiley-Liss, Inc.

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Documento generato il 04/07/20 alle ore 20:41:13