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Performance Comparison of the Experion Automated Electrophoresis System and a Competing Automated System for Protein Analysis, Rev A

otein 200 plus assay and bioanalyzer was less reproducible (CV of 19.0% and 18.2%) for the same two sample preparations. To further illustrate the difference in quantitation reproducibility for the two systems, all data points acquired for BSA quantitation were plotted (Figure 1). The clustering of the Pro260 assay data indicates that the interchip and intrachip reproducibility of quantitation by this assay was superior to that observed with the protein 200 plus assay.

For both protein analysis systems, the accuracy of relative quantitation was much greater for the BSA sample than for CA. The Pro260 assay produced deviations in quantitation of approximately 7% and 71% for BSA and CA, respectively, and the protein 200 plus assay quantitated these same two protein samples to within approximately 20% and 48% of the spectroscopically measured concentration (Table 2).

Such differences in quantitation accuracy for different proteins also occur with other commonly used protein quantitation methods, such as the Bradford and Lowry assays (bulletin 1069, Bradford 1976, Lowry et al. 1951), and are often due to differences in protein staining efficiency. Unique protein characteristics, such as primary sequence, amino acid composition, isoelectric point, and presence of modified amino acids and prosthetic groups, can affect the levels of staining and colorimetric signals produced. Both microfluidic systems perform quantitation using a single-point calibration to an internal upper marker protein; thus, relative quantitation accuracy is often highest for proteins that stain with similar efficiency to the upper marker protein.

Because proteins exhibit differences in staining behavior, an alterna
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