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Journal of Plant Biology

, Volume 50, Issue 2, pp 167–173 | Cite as

Mannose-binding lectin fromCurcuma zedoaria Rosc

  • Ponpimol Tipthara
  • Polkit Sangvanich
  • Marcus Macth
  • Amorn Petsom
Article

Abstract

A mannose-binding lectin was isolated from rhizomes of the medicinal plantCurcuma zedoaria. We used extraction with 20 mM phosphate buffer, ammonium sulfate precipitation, ion exchange chromatography on Q-Sepharose, gel filtration chromatography on Superdex 75, and reverse-phase HPLC. The purified lectin yielded a single band on SDS-PAGE that corresponded to a molecular mass of 13 kDa. This lectin exhibited hemagglutinating activity toward rabbit erythrocytes, which could be inhibited by mannose only. The lectin was digested with trypsin and its digests were analyzed using MALDI-TOF/TOF. Partial amino acid sequences were obtained from tandem mass spectra via automatedde novo sequencing, and were then identified by MS-BLAST homology searches to enable recognition of related proteins in other species. Inferred peptide sequences exhibited similarity to a mannose-binding lectin fromEpipactis helleborine, a member of the Orchidaceae.

Keywords

Curcuma zedoaria de novo sequencing hemagglutinating activity MALDI-TOF/TOF mannose-binding lectin 

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Copyright information

© The Botanical Society of Korea 2007

Authors and Affiliations

  • Ponpimol Tipthara
    • 1
  • Polkit Sangvanich
    • 1
  • Marcus Macth
    • 2
  • Amorn Petsom
    • 1
    • 3
  1. 1.Research Center for Bioorganic Chemistry, Department of ChemistryFaculty of Science, Chulalongkorn UniversityBangkokThailand
  2. 2.Bruker DaltonicsLeipzigGermany
  3. 3.Institute of Biotechnology and Genetic EngineeringChulalongkorn UniversityBangkok10330Thailand

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