The arylphorin (which came from incubated fat body) was mixed with a cold buffer. After centrifugation, the suspension was frozen and thawed; this denatured the contaminants which were then removed. The supernate was concentrated and then subjected to lectin affinity chromatography.
Most contaminating protein eluted with polyacrylamide slab gel electrophoresis with a buffer alone. Density scanning was used and showed that one fraction was highly contaminated. Fractions were pooled together to obtain about 98% arylphorin. The yield was about 30% of the initial total protein, which is a higher yield than in the original, unchanged procedure. Specific activity was determined after purification and then the precipitate was solubilized by heating prior to liquid scintillation counting.