Amino acid sequence of trichoanguina, a ribosomal-inactivating protein from Trichosanthes anguina seeds
Journal
Journal of Biomedical Science
Journal Volume
3
Journal Issue
3
Pages
178-186
Date Issued
1996
Author(s)
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 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.
Subjects
Protein sequence; Ribosome-inactivating protein(s); Trichoanguina; Trichosanthes anguina
SDGs
Other Subjects
abortive 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. anguina
Type
journal article