فهرست نشریات علمی دسترسی آزاد ایران

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.