Table 1.
The potential electron transfer components identified from affinity purification-mass spectrometry analysis of monolignol P450 enzymes
Bait ProteinProtein IdentifiedSpectral CountsUnique PeptidesPercentage Coverage
C4HCPR1536.8
CPR2212.1
CBR17418
CB5D7 (4)4 (3)41 (36)
CB5C4217
CB5E1 (2)1 (2)10 (28)
C3′HCPR1437.4
CPR2112.3
CBR15315
CB5D7 (1)4 (1)41 (9.3)
CB5C217.6
CB5E3216
F5HCPR1436.9
CPR2112.3
CBR15418
CB5D4 (2)2 (2)25 (24)
CB5C4217
CB5E2110
Bait ProteinProtein IdentifiedSpectral CountsUnique PeptidesPercentage Coverage
C4HCPR1536.8
CPR2212.1
CBR17418
CB5D7 (4)4 (3)41 (36)
CB5C4217
CB5E1 (2)1 (2)10 (28)
C3′HCPR1437.4
CPR2112.3
CBR15315
CB5D7 (1)4 (1)41 (9.3)
CB5C217.6
CB5E3216
F5HCPR1436.9
CPR2112.3
CBR15418
CB5D4 (2)2 (2)25 (24)
CB5C4217
CB5E2110

Purified proteins were subjected to SDS-PAGE, and the sliced gel pieces were processed for in-gel digestion and peptide elution (for data in parentheses), or the proteins were digested and eluted directly from protein-bound beads. The eluted peptides were injected for LC-MS analysis. The MS/MS data was searched with GPM X!Tandem software against the UniProt Arabidopsis database with P = 0.01.

Table 1.
The potential electron transfer components identified from affinity purification-mass spectrometry analysis of monolignol P450 enzymes
Bait ProteinProtein IdentifiedSpectral CountsUnique PeptidesPercentage Coverage
C4HCPR1536.8
CPR2212.1
CBR17418
CB5D7 (4)4 (3)41 (36)
CB5C4217
CB5E1 (2)1 (2)10 (28)
C3′HCPR1437.4
CPR2112.3
CBR15315
CB5D7 (1)4 (1)41 (9.3)
CB5C217.6
CB5E3216
F5HCPR1436.9
CPR2112.3
CBR15418
CB5D4 (2)2 (2)25 (24)
CB5C4217
CB5E2110
Bait ProteinProtein IdentifiedSpectral CountsUnique PeptidesPercentage Coverage
C4HCPR1536.8
CPR2212.1
CBR17418
CB5D7 (4)4 (3)41 (36)
CB5C4217
CB5E1 (2)1 (2)10 (28)
C3′HCPR1437.4
CPR2112.3
CBR15315
CB5D7 (1)4 (1)41 (9.3)
CB5C217.6
CB5E3216
F5HCPR1436.9
CPR2112.3
CBR15418
CB5D4 (2)2 (2)25 (24)
CB5C4217
CB5E2110

Purified proteins were subjected to SDS-PAGE, and the sliced gel pieces were processed for in-gel digestion and peptide elution (for data in parentheses), or the proteins were digested and eluted directly from protein-bound beads. The eluted peptides were injected for LC-MS analysis. The MS/MS data was searched with GPM X!Tandem software against the UniProt Arabidopsis database with P = 0.01.

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