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벼 렉틴 유전자의 플로닝 및 대장균에서의 발현

Molecular Cloning and Expression of Rice pectin Escherichia coli

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The lectin gene from rice was amplified by the polymerase chain reaction. The amplified DNA was inserted into the expression vector pET26b and expressed it as a fusion protein with polyhistidine sequences in Escherichia coli. The recombinant protein was produced by induction with 0.4 Mm isopropyl-β-D- thiogalactopyranoside at 37oC and purified by an immobilized metal affinity chromatography; The recombinant protein was found to have lectin activity by the hemag- glutination inhibition assay; The hemagglutination activity of the recombinant protein was optimal at pH 4.0-7.0 and was dependent on Ca2+ and Mn2+.

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