title: Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds.
abstract: In this study, we sequenced a new type I ribosome-inactivating protein, trichoanguina, from the seeds of Trichosanthes anguina (snake gourd). Trichoanguina is a basic glycoprotein having an apparent molecular mass of 35.0 kD and possessing strong ribosome-inactivating activity. Trichoanguina was cleaved with cyanogen bromide and partially digested with thermolysin, chymotrypsin, trypsin and Staphylococcus aureus V8 protease. The subsequent peptide fragments were separated by SDS-polyacrylamide gel electrophoresis, followed by electroblotting to polyvinylidene difluoride membranes and then sequencing. The sequencing of trichoanguina was completed, consisting of 245 amino acid residues. The sequencing of trichoanguina revealed a considerable homology to trichosanthin and alpha-trichosanthin, which are known as abortifacient, ribosome-inactivating and antihuman immunodeficiency virus proteins, with 46.7% and 55.6% amino acid identities, respectively. The sequence conserves two active sites: Glu-158 and Arg-161. Copyright 1996 S. Karger AG, Basel
authors.affiliation: Research Institute for Biosciences, Science University of Tokyo, Yamazaki, Noda, Japan.
authors.forename: L.-P.
authors.initials: LP
authors.lastname: Chow
authors.forename: M.
authors.initials: M
authors.lastname: Kamo
authors.forename: J.-Y.
authors.initials: JY
authors.lastname: Lin
authors.forename: S.-H.
authors.initials: SH
authors.lastname: Wang
authors.forename: Y.
authors.initials: Y
authors.lastname: Ueno
authors.forename: A.
authors.initials: A
authors.lastname: Tsugita