Purification and characterization of trichomaglin-a novel ribosomal-inactivating protein with abortificient activity.
Trichomaglin, a novel ribosome-inactivating protein, has been isolated from root tuber of a plant Maganlin (Trichosanthes Lepiniate, Cucurbitaceae). The isolation and purification procedure included ammonium sulfate precipitation, Sephadex G-75 chromatography and CM-Sephadex C-50 chromatography. The protein was identified to be homogeneous by SDS-PAGE and FPLC analysis. Its molecular weight is 24,673 dalton and isoelectric point is 5.8, determined by electrospray ionization mass spectroscopy and isoelectric focusing gel electrophoresis respectively. Trichomaglin can inhibit protein synthesis in rabbit reticulocyte lysate with ID50 of 10.1 nM. When rat ribosome was incubated with trichomaglin, a diagnostic RNA fragment appeared on polyacrylamide gel after ribosomal RNAs were treated with acidic aniline. It was concluded that trichomaglin is an RNA N-glycosidase. In addition, it has been verified to be an abortifacient protein.
http://www.ncbi.nlm.nih.gov/pubmed/10205663
Chen R, Xu YZ, Wu J, Pu Z, Jin SW, Liu WY, Xia ZX. Purification and characterization of trichomaglin-a novel ribosomal-inactivating protein with abortificient activity. Biochem Mol Biol Int. 1999 Feb;47(2):185-93.