LU-PING CHOWKamo M.Lin J.-Y.Wang S.-H.Ueno Y.Tsugita A.2020-01-222020-01-22199610217770https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029778772&partnerID=40&md5=5deaf6de89ba32648854a9ff580aea90https://scholars.lib.ntu.edu.tw/handle/123456789/452463In 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 α-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.Protein sequence; Ribosome-inactivating protein(s); Trichoanguina; Trichosanthes anguina[SDGs]SDG3abortive agent; anti human immunodeficiency virus agent; chymotrypsin; cyanogen bromide; glycoprotein; ribosome inactivating protein; thermolysin; trichoanguina; Trichosanthes extract; trichosanthin; trypsin; unclassified drug; amino acid sequence; article; nonhuman; plant seed; priority journal; protein degradation; sequence homology; Anguina; Cucurbita; Human immunodeficiency virus; Serpentes; Staphylococcus aureus; Trichosanthes; Trichosanthes cucumerina var. anguinajournal article2-s2.0-0029778772