YAKHAK HOEJI (약학회지)

The Pharmaceutical Society of Korea (대한약학회)
권호 표지

Molecular Cloning and Expression of Rice Lectin in Escherichia coli

벼 렉틴 유전자의 클로닝 및 대장균에서의 발현

  • 홍성관 (중앙대학교 자연과학대학 화학과) ;
  • 전상훈 (중앙대학교 자연과학대학 화학과) ;
  • 김하형 (중앙대학교 약학대학) ;
  • 공광훈 (중앙대학교 자연과학대학 화학과)
  • Published : 2002.08.01
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Abstract

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-$\beta$-D-thiogalactopyranoside at 37$^{\circ}C$ and purified by an immobilized metal affinity chromatography. The recombinant protein was found to have lectin activity by the hemagglutination inhibition assay. The hemagglutination activity of the recombinant protein was optimal at pH 4.0-7.0 and was dependent on $Ca^{2+}$ and Mn$^{2+}$.2+/.

Keywords

References

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