Abstract
Among the highly heterogeneous components of the mouse urinary protein complex (MUP) a hydrolase was detected which was capable of spliting the proteinase ester substrate TAME as well as a synthetic chromogenic tripeptide specific for tissue and urinary kallikreins. The binding of mouse-specific IgE antibodies from the serum of a highly mouse-allergic patient occurred preferentialy to this kallikrein-like enzyme. This finding underscores the possible association of significant biological activities with predominant IgE-binding allergens, especially in view of the strongly sensitizing potential and the known messenger functions of the MUP proteins.
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