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Chow LP, Kamo M, Lin JY, et al. Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds. J Biomed Sci. 1996;3(3):178-186doi: 10.1007/BF02253098.
Chow, L. P., Kamo, M., Lin, J. Y., Wang, S. H., Ueno, Y., & Tsugita, A. (1996). Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds. Journal of biomedical science, 3(3), 178-186. https://doi.org/10.1007/BF02253098
Chow, L.-P., et al. "Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds." Journal of biomedical science vol. 3,3 (1996): 178-186. doi: https://doi.org/10.1007/BF02253098
Chow LP, Kamo M, Lin JY, Wang SH, Ueno Y, Tsugita A. Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds. J Biomed Sci. 1996 May-Jun;3(3):178-186. doi: 10.1007/BF02253098. PMID: 11725098.
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J Biomed Sci. 1996 May-Jun;3(3):178-186. doi: 10.1007/BF02253098.

Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds.

Journal of biomedical science

L.-P. Chow, M. Kamo, J.-Y. Lin, S.-H. Wang, Y. Ueno, A. Tsugita

Affiliations

  1. Research Institute for Biosciences, Science University of Tokyo, Yamazaki, Noda, Japan.

PMID: 11725098 DOI: 10.1007/BF02253098

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

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