2010年11月
Detection of Rap1A as a yessotoxin binding protein from blood cell membranes
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
- 巻
- 20
- 号
- 22
- 開始ページ
- 6443
- 終了ページ
- 6446
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bmcl.2010.09.080
- 出版者・発行元
- PERGAMON-ELSEVIER SCIENCE LTD
As is the case with other ladder-shaped polyether compounds, yessotoxin is produced by marine dinoflagellate, and possesses various biological activities beside potent toxicity. To gain a better understanding of the molecular mechanism for high affinity between these polyethers and their binding proteins, which accounts for their powerful biological activities, we searched for its binding proteins from human blood cells by using the biotin-conjugate of desulfated YTX as a ligand. By a protein pull-down protocol with use of streptavidin beads, a band of specifically binding proteins was detected in SDS-PAGE. HPLC-tandem mass spectrometry (MS/MS) indicated that Rap 1A, one of Ras superfamily proteins, binds to the YTX-linked resins. Western blotting and surface plasmon resonance experiments further confirmed that Rap1A specifically binds to YTX with the K(D) value around 4 mu M. (C) 2010 Elsevier Ltd. All rights reserved.
- リンク情報
-
- DOI
- https://doi.org/10.1016/j.bmcl.2010.09.080
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/20943388
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000283052900020&DestApp=WOS_CPL
- URL
- http://orcid.org/0000-0001-7633-8495
- ID情報
-
- DOI : 10.1016/j.bmcl.2010.09.080
- ISSN : 0960-894X
- eISSN : 1464-3405
- ORCIDのPut Code : 58378946
- PubMed ID : 20943388
- Web of Science ID : WOS:000283052900020