Pokeweed Antiviral Protein (PAP), isolated from the leaves of the Phytolacca americana plant, is classified as a Ribosome Inactivating Protein (RIP). RIPs can depurinate rRNA and therefore can inhibit protein synthesis. It has been previously seen that an inactive form of PAP exists in vivo. This form could be the result of dimerization of PAP within the plant cell, prior to viral exposure.

The appearance of a PAP dimer has been confirmed through gel electrophoresis of the fractions collected of several PAP purifications. However, once the fractions are combined in order to determine concentration of the prep, the dimer dissociates. Here we present data as to whether or not PAP will form a dimer if subject to various conditions after initial purification.

Three factors that were studied were the concentration of the protein, potassium chloride concentration in the sample buffer, and pH of the sample buffer. After varying these conditions, the resultant fractions were separated using gel electrophoresis. Here we present the results of concentration of PAP via microcon, addition of buffer of various salt concentrations, and varying the pH of the sample buffer.