Isolation and partial characterization of nigrin b, a non-toxic novel type 2 ribosome-inactivating protein from the bark of Sambucus nigra L

Plant Mol Biol. 1993 Sep;22(6):1181-6. doi: 10.1007/BF00028990.

Abstract

The bark of Sambucus nigra L. contains a non-toxic novel type 2 ribosome-inactivating protein that we named nigrin b. In vitro, nigrin b strongly inhibited mammalian protein synthesis but did not affect plant nor bacterial protein synthesis. The protein (M(r) 58,000) contains two subunits, A (M(r) 26,000) and B (M(r) 32,000); linked by disulphide bridge(s). Nigrin b was found to be an rRNA N-glycosidase of the rRNA of intact mammalian ribosomes and shares a very good N-terminal amino-acid sequence homology with the anti-HIV-1 proteins TAP 29 and trichosanthin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Hemagglutination Tests
  • Molecular Sequence Data
  • N-Glycosyl Hydrolases / chemistry
  • N-Glycosyl Hydrolases / isolation & purification*
  • N-Glycosyl Hydrolases / pharmacology
  • Plant Proteins / isolation & purification*
  • Plant Proteins / pharmacology
  • RNA, Ribosomal / metabolism
  • Rabbits
  • Rats
  • Ribosome Inactivating Proteins
  • Ribosome Inactivating Proteins, Type 2
  • Ribosomes / drug effects*
  • Sequence Homology, Amino Acid
  • Trees / chemistry*

Substances

  • Plant Proteins
  • RNA, Ribosomal
  • Ribosome Inactivating Proteins, Type 2
  • N-Glycosyl Hydrolases
  • Ribosome Inactivating Proteins