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Mehran Miroliaei Samira Padidar Ali Moیtafaie Sirous Ghobad

Abstract

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.

Article Details

References
How to Cite
Mehran, M., Samira, P., Ali, M., & Sirous, G. (2010). Purification of Lipid Transfer Protein 2 (LTP2) from Iranian rice paddy. Journal of Cell and Molecular Research, 1(2), 72-76. https://doi.org/10.22067/jcmr.v1i2.3222
Section
Research Articles