Amino acid sequence of trichoanguina,a ribosomal-inactivating protein fromTrichosanthes anguina seeds |
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Authors: | Lu-Ping Chow Masaharu Kamo Jung-Yaw Lin Shiuan-Huei Wang Yoshio Ueno Akira Tsugita |
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Institution: | (1) Faculty of Pharmaceutical Sciences, Science University of Tokyo, Shinjuku, Tokyo, Japan;(2) Institute of Biochemistry, College of Medicine, National Taiwan University, Taipei, Taiwan;(3) Research Institute for Biosciences, Science University of Tokyo, 2669 Yamazaki, 278 Noda, Japan |
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Abstract: | In this study, we sequenced a new type I ribosome-inactivating protein, trichoanguina, from the seeds ofTrichosanthes 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 andStaphylococcus 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 anda-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. |
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Keywords: | Ribosome-inactivating protein(s) Trichosanthes anguina Trichoanguina Protein sequence |
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