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 o f mouse-specific IgE antibodies from the serum of a highly mouse-aller gic patient occurred preferentialy to this kallikrein-like enzyme. Thi s finding underscores the possible association of significant biologic al activities with predominant IgE-binding allergens, especially in vi ew of the strongly sensitizing potential and the known messenger funct ions of the MUP proteins.