Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10768300 | Biochemical and Biophysical Research Communications | 2005 | 6 Pages |
Abstract
Trichosanthin is a type I ribosome-inactivating protein with many pharmacological activities. The trichosanthin-coupled Sepharose affinity purification revealed a protein, which was identified by mass spectrometry as the ribosomal protein L10a. The interaction between trichosanthin and recombinant L10a was further confirmed by in vitro binding assay. Kinetic analysis by surface plasmon resonance technology revealed that L10a had a high affinity to trichosanthin with a KD of 7.78Â nM. The study with mutated forms of trichosanthin demonstrated that this specific association correlates with the ribosome-inactivating activity of trichosanthin. This finding might provide insight into the mechanisms by which trichosanthin inactivates ribosome and that underlies its pharmacological effect.
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Authors
Xuechun Xia, Fajian Hou, Jie Li, Huiling Nie,