Authentication email has already been sent, please check your email box: and activate it as soon as possible.
You can login to My Profile and manage your email alerts.
If you haven’t received the email, please:
|
|
There are 2 papers published in subject: > since this site started. |
Results per page: |
Select Subject |
Select/Unselect all | For Selected Papers |
Saved Papers
Please enter a name for this paper to be shown in your personalized Saved Papers list
|
1. Expression and purification of NSH2 domain protein for NMR research | |||
Niu Gao,Guo Jiangfeng,Zhang Yaozhou | |||
Biology 06 March 2009 | |||
Show/Hide Abstract | Cite this paper︱Full-text: PDF (0 B) | |||
Abstract:SHP-2 protein, which has two SH2 domains, is essential for the embryonic development, haematopoiesis and signaling downstream of a variety of growth factors. SHP-2 proteins are related to many diseases. To facilitate fundamental studies, it is important that the proteins can be expressed in high quality and in a large quantity. In this work, the amino-terminal SH2 (NSH2) domain of SHP-2 protein which is important for the protein’s self-regulation was recombinated into the prokaryotic expression vector, pGEX-2T, and introduced into E. coli BL21 for a prokaryotic expression. Two recombinant vectors with different extra amino acid residues were designed on the basis of properties of NSH2 protein and the sequence of expression vector, pGEX-2T, to produce NSH2 protein with a high property. The effects of the two groups of different extra amino acid residues on solubility and stability were compared. The comparisons indicated that end extra amino acid residues may have strong effects on both solubility and stability. The higher soluble and stable NSH2 protein was selected and labeled with isotope 15N for NMR study. The high resolution of NMR demonstrated the correction folding of the protein and the interactions of the protein with phosphop-tyrosin peptides. | |||
TO cite this article:Niu Gao,Guo Jiangfeng,Zhang Yaozhou. Expression and purification of NSH2 domain protein for NMR research[OL].[ 6 March 2009] http://en.paper.edu.cn/en_releasepaper/content/30007 |
2. Characterization of HMW Glutenin Subunits in Bread and Tetraploid Wheats by Reversed-Phase High-Performance Liquid Chromatography | |||
Dong Kun,Hao Chun-yan,Wang Ai-li,Cai Min-hua,Yan Yue-ming | |||
Biology 15 January 2009 | |||
Show/Hide Abstract | Cite this paper︱Full-text: PDF (0 B) | |||
Abstract:The wheat storage proteins, especially the high molecular weight glutenin subunits (HMW-GS), play important roles in the determination of flour processing and bread-making quality. Compared with the traditional SDS-PAGE method, reversed-phase high-performance liquid chromatography (RP-HPLC) was shown to have many advantages for the separation and characterization of HMW-GS because of its high resolving power, repeatability and automation. In this work, HMW-GS from bread and tetraploid wheats were separated and characterized by RP-HPLC. The elution time ranking of different HMW-GS was: 1Ax>1Bx>1Dx>1By>1Dy. Several subunit pairs associated with good quality properties and those with similar mobilities on SDS-PAGE, such as 1Bx7 and 1Bx7*, 1By8 and 1By8*, 1Dx2 and 1Ax2*, 1Bx6 and 1Bx6.1, were well separated and readily identified through RP-HPLC. However, other subunit pairs, such as 1Dy10-1Dy12, 1Dx5-1By18 and 1Dx2-1By16, could not be adequately separated and identified by RP-HPLC, whereas they displayed different mobilities on SDS-PAGE gels. Because 1Dx5 and 1Dx2 showed different hydrophobicities, RP-HPLC could distinguish 1Dx5+1Dy10 and 1Dx2+1Dy12. A comparative analysis between RP-HPLC and SDS-PAGE showed that a combination of both methods provided more effective identification of HMW-GS in wheat quality improvement and germplasm screening. | |||
TO cite this article:Dong Kun,Hao Chun-yan,Wang Ai-li, et al. Characterization of HMW Glutenin Subunits in Bread and Tetraploid Wheats by Reversed-Phase High-Performance Liquid Chromatography[OL].[15 January 2009] http://en.paper.edu.cn/en_releasepaper/content/27867 |
Select/Unselect all | For Selected Papers |
Saved Papers
Please enter a name for this paper to be shown in your personalized Saved Papers list
|
Results per page: |
About Sciencepaper Online | Privacy Policy | Terms & Conditions | Contact Us
© 2003-2012 Sciencepaper Online. unless otherwise stated