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Purification and characterization of trichomaglin ‐ A novel ribosome‐inactivating protein with abortifacient activity
Author(s) -
Chen Rong,
Xu Yongzhen,
Wu Jian,
Pu Zheng,
Jin Shanwei,
Liu Wangyi,
Xia Zongxiang
Publication year - 1999
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549900201193
Subject(s) - ribosome inactivating protein , ammonium sulfate precipitation , sephadex , chromatography , isoelectric point , chemistry , polyacrylamide gel electrophoresis , ribosome , fast protein liquid chromatography , gel electrophoresis , isoelectric focusing , biochemistry , size exclusion chromatography , rna , high performance liquid chromatography , enzyme , gene
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.