Expression and purification of the recombinant SALT lectin from rice ( Oryza sativa L.)
The SALT protein is a 14.5 kDa mannose-binding lectin, originally described as preferentially expressed in rice plant roots in response to NaCl stress. Recombinant SALT lectin was produced in Escherichia coli from a cDNA clone encoding protein. After isopropyl-β- d-thiogalactopyranoside induction, t...
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Veröffentlicht in: | Protein expression and purification 2004, Vol.33 (1), p.34-38 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The SALT protein is a 14.5
kDa mannose-binding lectin, originally described as preferentially expressed in rice plant roots in response to NaCl stress. Recombinant SALT lectin was produced in
Escherichia coli from a cDNA clone encoding protein. After isopropyl-β-
d-thiogalactopyranoside induction, the expression level achieved was 23% of the soluble protein. The recombinant agglutinin was purified by a single-step process by dialyses against a high concentrated salt solution. After purification, hemagglutination assays of rabbit erythrocytes revealed that the recombinant SALT protein is a potent agglutinin (0.078
μg
ml
−1 minimal concentration). The purified recombinant lectin was also used for comparative estimation of native protein amounts in protein extracts from rice plants by Western blot assay. |
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ISSN: | 1046-5928 1096-0279 |
DOI: | 10.1016/j.pep.2003.08.017 |