Purification of human erythrocyte adenosine deaminase

Abstract

In summary we have shown the following:1) Human erythrocyte ADA has been purified approximately 800,000 fold (sp. act. 538 micronmol/min/mg at 37 degrees) to apparent homogeneity using antibody affinity chromatography. 2) The enzyme was shown to be a single polypeptide chain with estimated molecular weight of approximately 38,000. 3) The 3 electrophoretic forms of erythrocyte ADA purified simultaneously by this technique were indistinguishable by SDS gel electrophoresis under reducing conditions. 4) Several properties of the highly purified ADA were identical to properties observed with an impure preparation of the enzyme.