Demonstration of ribonuclease activity in the plant ribosome-inactivating proteins alpha- and beta-momorcharins

J. W.Y. Mock, T. B. Ng, Ricky N S WONG, Q. Z. Yao, H. W. Yeung, W. P. Fong*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

66 Citations (Scopus)

Abstract

Alpha- and beta-momorcharins, ribosome-inactivating proteins from Momordica charantia seeds, were utilized in this investigation. Ribonucleolytic cleavage was observed after naked rRNA was incubated with either momorcharin. Beta-momorcharin, and to a lesser extent alpha-momorcharin, also acted on tRNA to release acid-soluble UV-absorbing products. Such activity was optimal at pH around 5.5. Using polyhomoribonucleotides as substrate, it was found that the momorcharins preferentially acted on polyU, but exerted negligible effects on polyA, polyC and polyG. Chromatographic analysis of the reaction product indicated that mono and/or oligo-ribonucleotides, but not free base, were generated from polyU, suggesting that the enzymatic action involved ribonucleolytic cleavage. Similar to the results obtained with tRNA as substrate, beta-momorcharin was about 15-fold more active than alpha-momorcharin on polyU.

Original languageEnglish
Pages (from-to)1853-1859
Number of pages7
JournalLife Sciences
Volume59
Issue number22
DOIs
Publication statusPublished - 25 Oct 1996

Scopus Subject Areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

User-Defined Keywords

  • Momordica charantia
  • ribonuclease
  • ribosome-inactivation proteins

Fingerprint

Dive into the research topics of 'Demonstration of ribonuclease activity in the plant ribosome-inactivating proteins alpha- and beta-momorcharins'. Together they form a unique fingerprint.

Cite this