Characterization of Mirabilis antiviral protein--a ribosome inactivating protein from Mirabilis jalapa L

Biochem Int. 1992 Dec;28(4):585-93.

Abstract

A protein was purified from root tubers of Mirabilis jalapa to homogeneity by ion-exchange chromatography on CM-Sepharose CL-6B and FPLC on Mono-S column. The purified protein was confirmed to be Mirabilis antiviral protein (MAP). However, in addition to its antiviral property, the MAP was demonstrated to possess abortifacient activity in pregnant mice, inhibitory effect on cell-free protein synthesis and antiproliferative effect on tumor cells. As judged from its biological and physiochemical properties, MAP is a type I ribosome-inactivating protein.

MeSH terms

  • Abortifacient Agents / isolation & purification
  • Abortifacient Agents / pharmacology
  • Animals
  • Antineoplastic Agents / isolation & purification
  • Antineoplastic Agents / pharmacology
  • Antiviral Agents / isolation & purification*
  • Antiviral Agents / pharmacology
  • Cell-Free System
  • Chromatography
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Humans
  • Mice
  • Mice, Inbred ICR
  • Molecular Weight
  • N-Glycosyl Hydrolases*
  • Plant Proteins / isolation & purification*
  • Plant Proteins / pharmacology
  • Plant Viruses / drug effects*
  • Plants / chemistry*
  • Plants / microbiology
  • Pregnancy
  • Protein Synthesis Inhibitors / isolation & purification*
  • Protein Synthesis Inhibitors / pharmacology
  • Ribosome Inactivating Proteins, Type 1
  • Tumor Cells, Cultured

Substances

  • Abortifacient Agents
  • Antineoplastic Agents
  • Antiviral Agents
  • Plant Proteins
  • Protein Synthesis Inhibitors
  • Ribosome Inactivating Proteins, Type 1
  • N-Glycosyl Hydrolases
  • MAP protein, Mirabilis jalapa