Several years ago Wattenberg and Glick noted that a purified nonspecific hyaluronidase inhibitor was blue in color and suggested that this pigment was ceruloplasmin.1 Further fractionation increased the potency of the inhibition tenfold but not the color as measured spectrophotometrically. On the basis of this observation the authors concluded that the enzyme-inhibiting factor probably was not related to the copper-bearing protein. The identity of the inhibitor and a heparin-like polysaccharide was suggested.
Later, Newman and his associates obtained a highly purified hyaluronidase inhibitor by a combination of chemical procedures and zone electrophoresis.2 No heparin was present, but the presence of glucosomine and uronic acid again suggested that the inhibitor might be polysaccharide. These investigators did not mention that their concentrated material had a blue color, nor did they report measurements of its copper content.
Kühnau3 has stated that copper in complex binding has a profound antihyaluronidase effect
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