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: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Ferdowsi University of Mashhad
2009-07-01
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| Series: | Journal of Cell and Molecular Research |
| Subjects: | |
| Online Access: | https://jcmr.um.ac.ir/article_25667_703fe450798ba03d9a503c42ea4cd0f0.pdf |
| _version_ | 1818976096800997376 |
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| author | Mehran Miroliaei Samira Padidar Ali Mostafaie Sirous Ghobadi |
| author_facet | Mehran Miroliaei Samira Padidar Ali Mostafaie Sirous Ghobadi |
| author_sort | Mehran Miroliaei |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-20T16:06:25Z |
| format | Article |
| id | doaj.art-d01cfb6e60484af3a911ae7e4702bb90 |
| institution | Directory Open Access Journal |
| issn | 2008-9147 2717-3364 |
| language | English |
| last_indexed | 2024-12-20T16:06:25Z |
| publishDate | 2009-07-01 |
| publisher | Ferdowsi University of Mashhad |
| record_format | Article |
| series | Journal of Cell and Molecular Research |
| spelling | doaj.art-d01cfb6e60484af3a911ae7e4702bb902022-12-21T19:34:08ZengFerdowsi University of MashhadJournal of Cell and Molecular Research2008-91472717-33642009-07-0112727610.22067/jcmr.v1i2.322225667Purification of Lipid Transfer Protein 2 (LTP2) from Iranian rice paddyMehran MiroliaeiSamira Padidar0Ali Mostafaie1Sirous Ghobadi2Razi UniversityRazi UniversityRazi UniversityAbstract 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.https://jcmr.um.ac.ir/article_25667_703fe450798ba03d9a503c42ea4cd0f0.pdfpurificationplant lipid transfer proteinscation-exchange chromatographyhydrophobic chromatography |
| spellingShingle | Mehran Miroliaei Samira Padidar Ali Mostafaie Sirous Ghobadi Purification of Lipid Transfer Protein 2 (LTP2) from Iranian rice paddy Journal of Cell and Molecular Research purification plant lipid transfer proteins cation-exchange chromatography hydrophobic chromatography |
| title | Purification of Lipid Transfer Protein 2 (LTP2) from Iranian rice paddy |
| title_full | Purification of Lipid Transfer Protein 2 (LTP2) from Iranian rice paddy |
| title_fullStr | Purification of Lipid Transfer Protein 2 (LTP2) from Iranian rice paddy |
| title_full_unstemmed | Purification of Lipid Transfer Protein 2 (LTP2) from Iranian rice paddy |
| title_short | Purification of Lipid Transfer Protein 2 (LTP2) from Iranian rice paddy |
| title_sort | purification of lipid transfer protein 2 ltp2 from iranian rice paddy |
| topic | purification plant lipid transfer proteins cation-exchange chromatography hydrophobic chromatography |
| url | https://jcmr.um.ac.ir/article_25667_703fe450798ba03d9a503c42ea4cd0f0.pdf |
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