Abstract
A β-glucuronidase inhibitor was isolated from human saliva by successive fractionation on DEAE-cellulose, Sephadex G-200 and DEAE-cellulose. Inhibition was non-competitive. The purity and homogeneity of the inhibitor was established by electrophoresis on cellulose-acetate membrane. The molecular weight of the inhibitor was determined to be 380,000 by Sephadex G-200 column chromatography. The inhibitor contained 46.7 per cent protein, 16.6 per cent hexose, 15.7 per cent hexosamine, 12.8 per cent sialic acid, and 4.9 per cent fucose. From the result of the immunoelectrophoresis against anti-human serum, the inhibitor seems to be derived from human serum, or it seems to have the same antigenic determinant as the serum components.
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