Purification of Lipid Transfer Protein 2 (LTP2) from Iranian rice paddy
محل انتشار: مجله سلول و تحقیقات مولکولی، دوره: 1، شماره: 2
سال انتشار: 1388
نوع سند: مقاله ژورنالی
زبان: فارسی
مشاهده: 458
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شناسه ملی سند علمی:
JR_JCMR-1-2_005
تاریخ نمایه سازی: 7 بهمن 1395
چکیده مقاله:
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 lipidsubstrates. In this communication a simple, rapid and low-cost alternative method was developed forpurification 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 aPhenyl-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.
کلیدواژه ها:
purification ، plant lipid transfer proteins ، cation-exchange chromatography ، hydrophobic chromatography
نویسندگان
Samira Padidar
Department of Biology, Faculty of Sciences, Razi University, Kermanshah, Iran
Mehran Miroliaei
Department of Biology, Faculty of Sciences, University of Isfahan, Isfahan, Iran
Ali Mostafaie
Medical Biology Research Center, Kermanshah University of Medical Science, Kermanshah, Iran
Sirous Ghobadi
Department of Biology, Faculty of Sciences, Razi University, Kermanshah, Iran