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A Rapid Method for the Purification of Analytical Grade Proteins From Plants Using Preparative SDS-PAGE and Preparative IEF

degree of purification that can be accomplished in a single run on the Model 491 Prep Cell. Fraction 36 of the Model 491 Prep Cell run shows sufficient purity and quantity (approximately 100 g total protein) suitable for direct amino acid sequence analysis. The data in Figure 2 demonstrate the advantage of using the Model 491 Prep Cell, compared to conventional chromatography techniques, as a quick means of obtaining protein suitable for sequence analysis. Those proteins (Figure 2) which were purified under native conditions, by conventional chromatography steps using an FPLC system, required additional lab time and cost but resulted in lower protein yields due to the extra steps.

Trying to further resolve fractions 3537 from the Model 491 Prep Cell run using preparative isoelectric focusing produced what appears to be a highly pure form of BiP in fraction 1 (Figure 2). However, this fraction had a pH of 3.05 which is approximately 2.2 pH units lower than that of BiP analysed on 2-D gels. We attribute this phenomenon to the probability that BiP still had SDS attached to it, thus causing it to migrate towards the cathode.

Here we have reported a quick method for the purification of protein suitable for both amino acid sequence analysis and antibody production. However, for a higher degree of resolution, we would recommend altering the Model 491 Prep Cell conditions by either increasing the elution rate from the Model 491 Prep Cell, or by decreasing the sample volume collected per fraction, or both. The previous recommendation should also prevent unnecessary loss of protein from additional purification steps.


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