Chemical Research in Chinese Universities ›› 2010, Vol. 26 ›› Issue (3): 427-430.

• Articles • Previous Articles     Next Articles

Easy-to-use Method to Display Arabidopsis Rubisco Interacting Proteins

SUN Li-wen1, LI Jian-hua2, LI Shan-yu3* and XI Jing-hui4*   

  1. 1. Key Lab for Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun 130021, P. R. China;
    2. Department of Engineering Chemistry, Mudanjiang University, Mudanjiang 157011, P. R. China;
    3. Department of Pediatrics, The First Hospital of Jilin University, Changchun 130021, P. R. China;
    4. College of Plant Science, Jilin University, Changchun 130062, P. R. China
  • Received:2009-07-15 Revised:2009-09-22 Online:2010-05-25 Published:2010-07-27
  • Contact: LI Shan-yu. E-mail: shanyul@sina.com; XI Jing-hui. E-mail: jhxi1965@jlu.edu.cn
  • Supported by:

    Supported by the National Natural Science Foundation of China(Nos.30470159 and C01020304).

Abstract:

Affinity-mediated protein separation is an integral part of proteomics, the most outstanding of which is immunoproteomics. However, in the immunoprecipitate system overwhelming Ab and Ag conceal Ag interacting proteins as the research targets, which is the rate-limiting step in the progress of comparative proteomic analyses. We presented a convenient and accurate method to tackle this problem. 1 mol/L NaCl elution buffer was applied to the complex Rubisco immunoprecipitate of Arabidopsis, the weakest force involved in the system was selectively broken up, resulting in the enrichment of Rubisco interacting proteins accessible for further comparative protein gel profile. The easy-to-use method sheds light on a narrow-down strategy supplement for comparative immunoproteomics.

Key words: Comparative proteomics; Arabidopsis; Rubisco; Immunoprecipitation