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source 15q superformance column  (Amersham Life Sciences Inc)

 
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    Amersham Life Sciences Inc source 15q superformance column
    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 <t>15Q</t> 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+.
    Source 15q Superformance Column, supplied by Amersham Life Sciences Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/source+15q+superformance+column/pmc01447468-75-13-21?v=Amersham+Life+Sciences+Inc
    Average 90 stars, based on 1 article reviews
    source 15q superformance column - by Bioz Stars, 2026-07
    90/100 stars

    Images

    1) Product Images from "Specific Modification of a Na + Binding Site in NADH:Quinone Oxidoreductase from Klebsiella pneumoniae with Dicyclohexylcarbodiimide † ‡ "

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

    Journal:

    doi: 10.1128/JB.188.9.3264-3272.2006

    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+.
    Figure Legend 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+.

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

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

    Techniques Used: Binding Assay



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    source 15q superformance column  (Amersham Life Sciences Inc)
    90
    Amersham Life Sciences Inc source 15q superformance column
    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 <t>15Q</t> 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+.
    Source 15q Superformance Column, supplied by Amersham Life Sciences Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/source+15q+superformance+column/pmc01447468-75-13-21?v=Amersham+Life+Sciences+Inc
    Average 90 stars, based on 1 article reviews
    source 15q superformance column - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    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+.

    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

    Identification of proteins in NDH-1 from the source 15Q chromatographic step a

    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