Ribosome inactivating protein and lectin from bitter melon (Momordica charantia) seeds: sequence comparison with related proteins

Biochem Biophys Res Commun. 1998 Dec 9;253(1):143-6. doi: 10.1006/bbrc.1998.9765.

Abstract

One of the ribosome inactivating proteins (RIPs), beta-momorcharin, and a lectin were isolated from seeds of the bitter melon Momordica charantia (Family Cucurbitaceae) in accordance with published procedures. Both beta-momorcharin and M. charantia lectin were then subjected to amino acid sequencing. beta-momorcharin exhibited considerable homology in sequence to other Cucurbitaceae RIPs, and also to the A chains of abrin and ricin which are type II (double-chained) RIPs. The resemblance between alpha-momorcharin and other RIPs is closer than that between beta-momorcharins and other RIPs. M. charantia lectin manifested a certain extent of sequence similarity to beta-momorcharin and other RIPs, and some degree of homology in sequence to lectins from Cucurbita maxima, Cucurbita argyrosperma, Sambucus nigra and Ricinus Communis.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Cucurbitaceae / chemistry*
  • Fruit / chemistry
  • Lectins / chemistry*
  • Molecular Sequence Data
  • Plant Lectins
  • Plant Proteins / chemistry*
  • Protein Synthesis Inhibitors / chemistry
  • Ribosomal Proteins*
  • Ribosome Inactivating Proteins
  • Ribosomes / drug effects
  • Ribosomes / metabolism*
  • Seeds / chemistry*
  • Sequence Homology, Amino Acid*

Substances

  • Lectins
  • Plant Lectins
  • Plant Proteins
  • Protein Synthesis Inhibitors
  • Ribosomal Proteins
  • MMC protein, Momordica charantia
  • Ribosome Inactivating Proteins