Protein affinity chromatography three-dimensional structures

High-scale purification methods are required for several protein studies such as crystallography, mass specttometty, circular dichroism, and function. Here we describe a purification method for PAP based on anion exchange, L-(+)-tartrate affinity, and gel filtration chromatographies. Acid phosphatase activity and protein concentration were measured for each purification step, and to collect the firactions with the highest acid phosphatase activity the p-nittophenyl phosphate method was used. The purified protein obtained by the procediue described here was used for the determination of the first reported three-dimensional structure of prostatic add phosphatase. 

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