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Structural characterization and comparative modeling of PD-Ls 1e3, type 1 ribosome-inactivating proteins from summer leaves of Phytolacca dioica L.

Tipo de material: TextoTextoSeries ; Biochimie, 91, p.352-363, 2009Trabajos contenidos:
  • Di Maro, A
  • Chambery, A
  • Carafa, V
  • Costantini, S
  • Colonna, G
  • Parente, A
Tema(s): Recursos en línea: Resumen: 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
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Documentos solicitados Documentos solicitados CICY Documento préstamo interbibliotecario Ref1 B-12739 (Browse shelf(Opens below)) Available

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

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