English  |  正體中文  |  简体中文  |  Items with full text/Total items : 28607/40644
Visitors : 5919779      Online Users : 284
RC Version 4.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Adv. Search

Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/29362

Title: Isolation and Characterization of the Female-Specific Protein (Vitellogenin) in Mature Female Hemolymph of the Freshwater Prawn,Macrobrachium rosenbergii:Comparison with Ovarian Vitellin
Authors: Fang-Yi Lee;Tung-Wei Shih;Ching-Fong Chang
Contributors: NTOU:Institute of Marine Biology
Date: 1997-12
Issue Date: 2011-10-21T03:05:28Z
Publisher: General and Comparative Endocrinology
Abstract: 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 considered as 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 bonds were 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 in a few amino acids. Eight amino acid sequences from the N-terminal end of 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 precipitation in a solution with low ionic strength than vitellin. This study suggests a close relationship between vitellogenin and vitellin inM. rosenbergiiin their biochemical characteristics.
Relation: 108(3), pp.406–415
URI: http://ntour.ntou.edu.tw/handle/987654321/29362
Appears in Collections:[海洋生物研究所] 期刊論文

Files in This Item:

File Description SizeFormat

All items in NTOUR are protected by copyright, with all rights reserved.


著作權政策宣告: 本網站之內容為國立臺灣海洋大學所收錄之機構典藏,無償提供學術研究與公眾教育等公益性使用,請合理使用本網站之內容,以尊重著作權人之權益。
網站維護: 海大圖資處 圖書系統組
DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback