Journal
PROTEOMICS
Volume 6, Issue 21, Pages 5683-5687Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/pmic.200600267
Keywords
mitochondria; paper bridge loading; two-dimensional gel electrophoresis
Funding
- NHLBI NIH HHS [P01 HL077180-050001, P01 HL081427-040003, P01 HL081427-010003, P50 HL084946-029003, N0-HV-28120, P01 HL077180-010001, P01 HL077180, P01 HL081427-030003, P01 HL081427, P01 HL077180-020001, P01 HL081427-050003, P01HL081427, P50 HL084946, P01HL077180, P50 HL084946-019003, P50 HL084946-039003, P01 HL077180-040001, P01 HL077180-030001, P01 HL081427-020003] Funding Source: Medline
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Separation of basic proteins with 2-DE presents technical challenges involving protein precipitation, load limitations, and streaking. Cardiac mitochondria are enriched in basic proteins and Revised: June 12, 2006 difficult to resolve by 2-DE. We investigated two methods, cup and paper bridge, for sample Accepted: June 19, 2006 loading of this subproteome into the basic range (pH 6-11) gels. Paper bridge loading consistently produced improved resolution of both analytical and preparative protein loads. A unique benefit of this technique is that proteins retained in the paper bridge after loading basic gels can be reloaded onto lower pH gradients (pH 4-7), allowing valued samples to be analyzed on multiple pH ranges.
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