中國醫藥大學機構典藏 China Medical University Repository, Taiwan:Item 310903500/29979
English  |  正體中文  |  简体中文  |  Items with full text/Total items : 29490/55136 (53%)
Visitors : 1522744      Online Users : 360
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version
    CMUR > China Medical University Hospital > Jurnal articles >  Item 310903500/29979
    Please use this identifier to cite or link to this item: http://ir.cmu.edu.tw/ir/handle/310903500/29979


    Title: Bilateral simultaneous tubal sextuplets: pregnancy after in-vitro fertilization-embryo transfer following salpingectomy
    Authors: Chang, CC;Wu, TH;Tsai, HD;Lo, HY
    Contributors: 附設醫院婦產部;China Med Coll Hosp, Dept Obstet & Gynecol, Invitro Fertilizat Unit, Taichung, Taiwan
    Date: 1998
    Issue Date: 2010-09-24 14:47:03 (UTC+8)
    Publisher: OXFORD UNIV PRESS
    Abstract: Syncephapepsin is a fungal aspartic proteinase from Syncephalastrum racemosum. By using the property of syncephapepsin after having increased activity at higher temperature, two rapid purification protocols were developed, In the former case, a crude extract was initially diluted fivefold with an activity assay buffer and heated at 50 degrees C overnight, In this situation, syncephapepsin would digest most of the proteins that the crude extract contained, Subsequently, syncephapepsin of the crude extract was precipitated from 50 to 70% of ammonium sulfate and the preparation was then directly applied to the Superdex 200 HR FPLC column. In this manner, syncephapepsin was rapidly purified to apparent homogeneity within 24 h. In this report, an alternative method of purification is also provided, Compared with the procedure mentioned above, the heating step was proceeded after FPLC chromatography through which the same result was obtained. Using cytochrome c and RNase A as substrates, the cleavage sites of both substrates were identified by HPLC peptide mapping. The results showed that syncephapepsin had a broad specificity. Residues recognized to be cleaved were primarily those of trypsin and chymotrypsin and Lys was the most susceptible, (C) 1998 Academic Press.
    Relation: HUMAN REPRODUCTION 13(3):762-765
    Appears in Collections:[China Medical University Hospital] Jurnal articles

    Files in This Item:

    There are no files associated with this item.



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

     


    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback