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The purification of an enzyme is described, a protease, from human erythrocytes which degrades insulin with a high specificity at physiological hormone concentrations. Since the enzyme contains free sulfhydryl groups, affinity chromatography on organomercuri-Sepharose proved to be applicable as a valuable step in the isolation procedure. The purification factor amounted to approx. 6000, the yield to 8%. 1mg of purified enzyme was capable of degrading 50 pmol of insulin/min into trichloroacetic acid-soluble split products. The purified insulin-degrading enzyme was shown to be homogeneous, as demonstrated by gel chromatography, gel electrophoresis and isoelectric focusing. The isoelectric points was at pH 5.8. The molecular  weight of nativ enzyme was estimated by gel chromatography and gel electrophoresis and found to be about 150 000-160 000, consisting of 4 subunits. Degradation products of insulin eluted from a Biogel P 30 column are smaller than the A-chain of the hormone, suggesting the activity of a protease. The enzyme appears to be specific for insulin in that it does not degrade other peptide hormones such as growth hormone, prolactin, or thyroid-stimulating hormone. Furthermore, the enzyme does not inactivate enzymes such as lactate dehydrogenase, aldolase, fructose 1,6-bisphosphatase, hexosephosphate isomerase or hexokinase.

Purification to Homogeneity of an Insulin-Degrading Enzyme from Human Erythrocytes