Purification and characterization of trichomaglin--a novel ribosome-inactivating protein with abortifacient activity.
Biochem Mol Biol Int
; 47(2): 185-93, 1999 Feb.
Article
em En
| MEDLINE
| ID: mdl-10205663
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
/
Ribossomos
/
Abortivos não Esteroides
/
Cucurbitaceae
/
N-Glicosil Hidrolases
Limite:
Animals
Idioma:
En
Ano de publicação:
1999
Tipo de documento:
Article