An IgE-binding TAME esterase in the urine of the mouse, Mus musculus domesticus.

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 preferentially 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.