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Titolo:
ISOLATION AND CHARACTERIZATION OF THE FEMALE-SPECIFIC PROTEIN (VITELLOGENIN) IN MATURE FEMALE HEMOLYMPH OF THE FRESH-WATER PRAWN, MACROBRACHIUM-ROSENBERGII - COMPARISON WITH OVARIAN VITELLIN
Autore:
LEE FY; SHIH TW; CHANG CF;
Indirizzi:
NATL TAIWAN OCEAN UNIV,DEPT AQUACULTURE CHILUNG 20224 TAIWAN NATL TAIWAN OCEAN UNIV,DEPT AQUACULTURE CHILUNG 20224 TAIWAN
Titolo Testata:
General and comparative endocrinology
fascicolo: 3, volume: 108, anno: 1997,
pagine: 406 - 415
SICI:
0016-6480(1997)108:3<406:IACOTF>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRAYFISH IBACUS-CILIATUS; MALACOSTRACAN CRUSTACEA; ARMADILLIDIUM-VULGARE; TERRESTRIAL ISOPOD; PENAEUS-CHINENSIS; WATER PRAWN; PURIFICATION; YOLK; LIPOVITELLIN; ABLATION;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
F.Y. Lee et al., "ISOLATION AND CHARACTERIZATION OF THE FEMALE-SPECIFIC PROTEIN (VITELLOGENIN) IN MATURE FEMALE HEMOLYMPH OF THE FRESH-WATER PRAWN, MACROBRACHIUM-ROSENBERGII - COMPARISON WITH OVARIAN VITELLIN", General and comparative endocrinology, 108(3), 1997, pp. 406-415

Abstract

Purification and characterization of the female-specific protein (vitellogenin) from the hemolymph of mature female prawn, Macrobrachium rosenbergii, were the objectives of this study. The comparison of biochemical characteristics between vitellogenin and ovarian vitellin was also conducted. Hemolymph vitellogenin was purified with DEAE, hydroxylapatite, and another DEAE chromatographic column. The specific protein (vitellogenin) was shown in the fractions of chromatographic columns on the basis of ELISA, Western blotting, and immunoprecipitation. A purified vitellogenin was obtained with an apparent molecular weight of 700 kDa as determined by PAGE. The purified vitellogenin was consideredas a lipoglycoprotein on the basis of staining data. Three subunits (170, 100, and 89 kDa) in purified vitellogenin and two subunits (100 and 89 kDa) in vitellin were detected with SDS-PAGE. Nondisulfide bondswere found in the binding of polypeptide subunits. Only the 89-kDa subunit was a glycopolypeptide in both vitellogenin and vitellin. The amino acid composition of vitellogenin differed from that of vitellin ina few amino acids. Eight amino acid sequences from the N-terminal endof 89- and 100-kDa subunits were determined and they were identical between vitellogenin and vitellin. Seven amino acid sequence from the N-terminal end of the 170-kDa subunit were also identical to the 100-kDa subunit. Purified vitellogenin was more susceptible to precipitationin a solution with low ionic strength than vitellin. This study suggests a close relationship between vitellogenin and vitellin in hi. rosenbergii in their biochemical characteristics. (C) 1997 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 05:59:57