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- Title
CLONING, EXPRESSION AND CHARACTERIZATION OF NOVEL LECTIN FROM ORYZA SATIVA.
- Authors
KWANG-HOON ONG; SUNG-GUAN HONG; SUN-YOUNG YOO; KWANG-SOO LEE; HA-HYUNG KIM
- Abstract
A lectin gene homolog of Oryza sativa was successfully cloned and expressed in Escherichia coli . The deduced amino acid sequence of the protein product showed a significant similarity with known chitin-binding lectins. Most of the recombinant lectin was found in an insoluble aggregated form as inclusion bodies and only a small part was in the culture medium in a soluble active form. Functional recombinant lectin was recovered from the inclusion bodies by solubilization with 8 M urea in Tris/HCl buffer, pH 7.0 and renaturation by 10-fold dilution in the same buffer. The recombinant lectin with His-tag was simply purified to homogeneity by the process of affinity chromatography and was obtained with a yield of 6–8 mg/L culture. The recombinant lectin was a homo-dimer composed of 22 kDa. The hemagglutination activity of the recombinant lectin was optimal at pH 4.0–7.0 and it was very sensitive to inhibition by N -acetylneuraminic acid and thyroglobulin.
- Subjects
RICE; ORYZA; LECTINS; CLONING; GENE expression; ESCHERICHIA coli; AMINO acid sequence
- Publication
Journal of Food Biochemistry, 2004, Vol 28, Issue 6, p500
- ISSN
0145-8884
- Publication type
Article
- DOI
10.1111/j.1745-4514.2004.06303.x