Purification of Lipid Transfer Protein 2 (Ltp2) From Iranian Rice Paddy

Plant nonspecific lipid transfer proteins (nsltps) are divided into nsltp1 and nsltp2. the existence of aninternal 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-sepharosecolumn, 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 ionexchangecolumn, showed multiple bands in the range of 2-20 kda. further purification using hydrophobiccolumn resulted in single band of nsltp2 at about 7 kda, reflecting a purified sample in the gel.