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Characterization of the enzymatic mechanism of gamma-momorcharin, a novel ribosome-inactivating protein with lower molecular weight of 11,500 purified from the seeds of bitter gourd (Momordica charantia).

Abstract：

:The enzymatic mechanism of a small ribosome-inactivating protein, gamma-momorcharin, purified from the seeds of Momordica charantia, has been characterized. By SDS-polyacrylamide and electrospray ionization mass spectrometry, its molecular weight was measured to be 11,500 daltons which is much lower than other RIPs known to date. It can inhibit the protein synthesis in the rabbit reticulocyte cell-free system with ID50 of 55 nM. When rat liver ribosome was incubated with gamma-momorcharin, a diagnostic RNA fragment appeared on the gel after rRNAs were treated with acid aniline. Sequencing of the RNA fragment indicates that the action site of gamma-momorcharin in 28S ribosomal RNA of rat liver is at a specific adenosine (position 4324), which is in a highly conserved loop of 28S rRNA.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Pu Z,Lu BY,Liu WY,Jin SW

doi

10.1006/bbrc.1996.1794

subject

Has Abstract

pub_date

1996-12-04 00:00:00

pages

287-94

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)91794-5

journal_volume

229

pub_type

杂志文章

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