Ribosome-inactivating lectins with polynucleotide:adenosine glycosidase activity

FEBS Lett. 1997 May 26;408(3):355-9. doi: 10.1016/s0014-5793(97)00463-8.

Abstract

Lectins from Aegopodium podagraria (APA), Bryonia dioica (BDA), Galanthus nivalis (GNA), Iris hybrid (IRA) and Sambucus nigra (SNAI), and a new lectin-related protein from Sambucus nigra (SNLRP) were studied to ascertain whether they had the properties of ribosome-inactivating proteins (RIP). IRA and SNLRP inhibited protein synthesis by a cell-free system and, at much higher concentrations, by cells and had polynucleotide:adenosine glycosidase activity, thus behaving like non-toxic type 2 (two chain) RIP. APA and SNAI had much less activity, and BDA and GNA did not inhibit protein synthesis.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Animals
  • Cell Line
  • Cell-Free System
  • Galanthus
  • HeLa Cells
  • Humans
  • Kinetics
  • Lectins / metabolism*
  • Lectins / pharmacology
  • Mice
  • Plant Lectins
  • Protein Synthesis Inhibitors / pharmacology*
  • Ribosome Inactivating Proteins
  • Ribosomes / metabolism*

Substances

  • Lectins
  • Plant Lectins
  • Protein Synthesis Inhibitors
  • Sambucus nigra lectins
  • Ribosome Inactivating Proteins