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Efficient Cleavage of Fusion Proteins to Yield Native Amino Termini

esis ((SDS-PAGE).). As the results in figure 2 indicate, after a 21-hour incubation, all of the fusion protein is cleaved in the absence of any detectable nonspecific proteolytic activity.

Figure 3

Following purification of fusion proteins and proteolytic removal of the affinity peptide tags, recombinant EK reactions contain a mixture of the protein of interest, the free affinity tag, recombinant EK and, occasionally, small amounts of uncleaved fusion protein. Recovery of the mature cleavage product from this mixture is often desired. Figure 3 (Panel A) shows the results of a simple and efficient one-step protocol for removing both recombinant EK and products that contain the CBP affinity tag. In the first experiment, the fusion protein was briefly digested with recombinant EK to yield a mixture of uncleaved fusion protein, mature JNK cleavage product and the free CBP tag (lane 2). The reaction was absorbed for 30 minutes with a mixed slurry of CaM affinity resin and STI Agarose (the latter is for the removal of recombinant EK, not visible on the gel). In this experiment, all of the detectable fusion protein and CBP were bound to the resin (lane 4), while the vast majority of the JNK cleavage product remained in the unbound fraction (lane 3). In a separate experiment, (Panel B) a reaction containing an excess of recombinant EK (200 ng) was split and absorbed with either CaM affinity resin alone (STI, +CaM) or with a mixed slurry of CaM affinity resin and STI Agarose (+STI, +CaM), and the unbound material was assayed for the presence of recombinant EK activity using a fluorescent
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