Purification and characterization of three mitogenic lectins from the roots of pokeweed (Phytolacca americana)

Biosci Biotechnol Biochem. 1995 Apr;59(4):683-8. doi: 10.1271/bbb.59.683.

Abstract

Three mitogenic lectins, designated PL-A, PL-B, and PL-C, were purified from the roots of pokeweed (Phytolacca americana) using Q-Sepharose column chromatography followed by gel filtration on Sephadex G-75, hydrophobic chromatography on Butyl-Toyopearl, and FPLC on a Mono-Q column. PL-A, PL-B, and PL-C are acidic proteins having isoelectric points of 4.35 and their apparent molecular masses were 22, 48, and 21 kDa by SDS-polyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol, respectively. The three lectins have similar amino acid compositions rich in half-cystine and similar N-terminal sequences, indicating that they are homologous proteins. Identical sequences of N-terminal regions and six corresponding tryptic peptides in PL-A and PL-B suggested that PL-A may be an N-terminal half fragment of PL-B. Although all of three lectins have mitogenic activities, PL-B is a mitogenic lectin with the most potent hemagglutinating and mitogenic activities, and PL-C has almost no hemagglutinating activity.

MeSH terms

  • Amino Acid Sequence
  • Cells, Cultured
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Electrophoresis, Polyacrylamide Gel
  • Erythrocytes / drug effects
  • Hemagglutination Tests
  • Humans
  • Molecular Sequence Data
  • Peptide Mapping
  • Plant Lectins
  • Plant Roots / chemistry
  • Pokeweed Mitogens / chemistry
  • Pokeweed Mitogens / isolation & purification*
  • Pokeweed Mitogens / pharmacology
  • Trypsin

Substances

  • Plant Lectins
  • Pokeweed Mitogens
  • Trypsin