PMID:11878806

Citation	Grady, JK, Zang, J, Laue, TM, Arosio, P and Chasteen, ND (2002) Characterization of the H- and L-subunit ratios of ferritins by sodium dodecyl sulfate-capillary gel electrophoresis. Anal. Biochem. 302:263-8
Abstract	Sodium dodecyl sulfate-capillary gel electrophoresis (SDS-CGE) was used to characterize the H- and L-subunit ratios of several mammalian ferritins and one bacterioferritin. Traditionally, SDS-PAGE has been used to characterize the H- and L-subunit ratios in ferritin; however, this technique is relatively slow and requires staining, destaining, and scanning before the data can be processed. In addition, the H- and L-subunits of ferritin are fairly close in molecular weight (approximately 21,000 and approximately 20,000, respectively) and are often difficult to resolve in SDS-PAGE slab gels. In contrast, SDS-CGE requires no staining or destaining procedures and the peak quantitation is superior to SDS-PAGE. SDS-CGE is effective in quickly resolving the H- and L-subunits of ferritins from horse spleen, human liver, recombinant human H and L homopolymers, and mixtures of the two- and the single-subunit of a bacterioferritin from Escherichia coli. The technique has also proven useful in assaying the quality of the protein sample from both commercial and recombinant sources. Significant amounts of low-molecular-weight degradation products were detected in all commercial sources of horse spleen ferritin. Most commercial horse spleen ferritins lacked intact H-subunits under denaturing conditions.
Links	PubMed Online version:10.1006/abio.2001.5561
Keywords	Animals; Bacterial Proteins; Cytochrome b Group/analysis; Electrophoresis, Capillary/methods; Electrophoresis, Polyacrylamide Gel/methods; Escherichia coli; Ferritins/analysis; Horses; Humans; Protein Subunits; Recombinant Proteins/analysis
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