Purification of Lipid Transfer Protein 2 (LTP2) from Iranian rice paddy
Abstract Plant nonspecific lipid transfer proteins (nsLTPs) are divided into nsLTP1 and nsLTP2. The existence of an internal hydrophobic cavity, is a typical characteristic of nsLTPs that serves as the binding site for lipid substrates. In this communication a simple, rapid and low-cost alternative...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Ferdowsi University of Mashhad
2009-07-01
|
| Series: | Journal of Cell and Molecular Research |
| Subjects: | |
| Online Access: | https://jcmr.um.ac.ir/article_25667_703fe450798ba03d9a503c42ea4cd0f0.pdf |
| Summary: | Abstract
Plant nonspecific lipid transfer proteins (nsLTPs) are divided into nsLTP1 and nsLTP2. The existence of an
internal hydrophobic cavity, is a typical characteristic of nsLTPs that serves as the binding site for lipid
substrates. In this communication a simple, rapid and low-cost alternative method was developed for
purification of nsLTP2 from rice paddy. After extracting, final supernatant was loaded on CM-Sepharose
column, which had previously equilibrated with 0.05 M Tris-HCl buffer, pH 8. Bounded proteins were
separated using a linear gradient of 0-0.5 M NaCl. Solution of separated proteins was dialyzed and applied on a
Phenyl-Sepharose column which previously equilibrated with Tris-HCl 0.05 M, ammonium sulfate 1.5 M,
EDTA 0.005 M and NaHSO3 0.3%, pH 8.4. Tris-Tricin SDS-PAGE of separated proteins, obtained from ionexchange
column, showed multiple bands in the range of 2-20 kDa. Further purification using hydrophobic
column resulted in single band of nsLTP2 at about 7 kDa, reflecting a purified sample in the gel. |
|---|---|
| ISSN: | 2008-9147 2717-3364 |