Elsevier

Phytochemistry

Volume 33, Issue 5, 23 July 1993, Pages 979-983
Phytochemistry

Purification and characterization of a tuber lectin from Alocasia indica

https://doi.org/10.1016/0031-9422(93)85007-EGet rights and content

Abstract

A lectin from the tubers of Alocasia indica Schott has been purified by affinity chromatography on asialofetuin-linked amino activated silica beads. The bound lectin was eluted with 0.1 M glycine-HC1 buffer, pH 2.5. The purified lectin yielded a single band on SDS-PAGE, pH 8.3, corresponding to M1 of 13 000. In polyacrylamide gel electrophoresis, pH 4.5, and gel exclusion chromatography, it also gave a single band and a single peak, respectively, with M1 of 55 000. However, in polyacrylamide gel electrophoresis at pH 8.3, it revealed three bands. Three peaks were obtained when the affinity purified lectin was applied on a DEAE-5PW HPLC analytical column. As a haemagglutinin, this lectin was effective against animal but not human erythrocytes. The haemagglutination activity is inhibited by asialofetuin only. The purified lectin is a glycoprotein with 1.47% carbohydrate content and has no metal ion requirement for its haemagglutinating activity. Alocasia indica was found to be mi togenic for human peripheral blood lymphocytes.

References (27)

  • R. Lotan et al.

    Biochim. Biophys. Acta.

    (1979)
  • C. Pena et al.

    Phytochemistry

    (1988)
  • C.E. Hayes et al.

    J. Biol. Chem.

    (1974)
  • J. Petryniak et al.

    Arch. Biochem.

    (1977)
  • R.G. Spiro et al.

    J. Biol. Chem.

    (1974)
  • B. Nilsson et al.

    J. Biol. Chem.

    (1979)
  • J.K. Bryan

    Analyt. Biochem.

    (1977)
  • O.H. Lowry et al.

    J. Biol. Chem.

    (1951)
  • R.G. Spiro
  • M. Paulova et al.

    Biochim. Biophys. Acta

    (1971)
  • I.J. Goldstein et al.

    Nature

    (1980)
  • J. Kocourek et al.
  • D. Renaur et al.

    Analyt. Biochem.

    (1985)
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