Journal:

Article Title: Specific Modification of a Na + Binding Site in NADH:Quinone Oxidoreductase from Klebsiella pneumoniae with Dicyclohexylcarbodiimide † ‡

doi: 10.1128/JB.188.9.3264-3272.2006

Figure Lengend Snippet: Identification of proteins in NDH-1 and modification of subunit NuoH with [14C]DCCD. Panel A shows the SDS-PAGE of NDH-1 (100 μg) after Source 15Q chromatography (lane 1) and the 2-butanol extract from 2 mg NDH-1 (lane 2). The gels were stained with Coomassie. Polypeptides were identified by mass spectroscopy (see Table ​Table11 for results) or N-terminal sequencing (indicated with an asterisk). Nuo and Atp denote subunits of NDH-1 and the F1Fo ATPase, respectively. Panel B shows the autoradiograms of NDH-1 after modification with [14C]DCCD and separation by SDS-PAGE. Two aliquots of NDH-1 (30 μg each) were mixed with [14C]DCCD in the presence of 0.6 mM Na+ (lane 3) or 50 mM Na+ (lane 4). Lane 5 shows the autoradiogram of the 2-butanol extract from 2 mg NDH-1 after modification with [14C]DCCD in the presence of 0.6 mM Na+.

Article Snippet: The concentrated NDH-1 was resuspended in 1.5 ml buffer and loaded onto a Source 15Q Superformance column (1.6 by 2 cm; Amersham).

Techniques: Modification, SDS Page, Chromatography, Staining, Mass Spectrometry, Sequencing

Journal:

Article Title: Specific Modification of a Na + Binding Site in NADH:Quinone Oxidoreductase from Klebsiella pneumoniae with Dicyclohexylcarbodiimide † ‡

doi: 10.1128/JB.188.9.3264-3272.2006

Figure Lengend Snippet: Identification of proteins in NDH-1 from the source 15Q chromatographic step a

Article Snippet: The concentrated NDH-1 was resuspended in 1.5 ml buffer and loaded onto a Source 15Q Superformance column (1.6 by 2 cm; Amersham).

Techniques: Binding Assay