Structural characterization and comparative modeling of PD-Ls 1e3, type 1 ribosome-inactivating proteins from summer leaves of Phytolacca dioica L.
Structural characterization and comparative modeling of PD-Ls 1e3, type 1 ribosome-inactivating proteins from summer leaves of Phytolacca dioica L.
- Biochimie, 91, p.352-363, 2009 .
The amino acid sequence and glycan structure of PD-L1, PD-L2 and PD-L3, type 1 ribosome-inactivating proteins isolated from Phytolacca dioica L. leaves, were determined using a combined approach based on peptide mapping, Edman degradation and ESI-Q-TOF MS in precursor ion discovery mode. The comparative analysis of the 261 amino acid residue sequences showed that PD-L1 and PD-L2 have identical primary structure, as it is the case of PD-L3 and PD-L4. Furthermore, the primary structure of PD-Ls 1e2 and PD-Ls 3e4 have 81.6
RIBOSOME-INACTIVATING PROTEINS
PHYTOLACCA DIOICA
EDMAN DEGRADATION
ESI-Q-TOF MASS SPECTROMETRY
COMPARATIVE MODELING
The amino acid sequence and glycan structure of PD-L1, PD-L2 and PD-L3, type 1 ribosome-inactivating proteins isolated from Phytolacca dioica L. leaves, were determined using a combined approach based on peptide mapping, Edman degradation and ESI-Q-TOF MS in precursor ion discovery mode. The comparative analysis of the 261 amino acid residue sequences showed that PD-L1 and PD-L2 have identical primary structure, as it is the case of PD-L3 and PD-L4. Furthermore, the primary structure of PD-Ls 1e2 and PD-Ls 3e4 have 81.6
RIBOSOME-INACTIVATING PROTEINS
PHYTOLACCA DIOICA
EDMAN DEGRADATION
ESI-Q-TOF MASS SPECTROMETRY
COMPARATIVE MODELING