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.
Berrens
L
L
Research Laboratories, CBF LETI, Madrid, Spain.
D000510:Alpha-Globulins / Q000737:chemistry* / Q000276:immunology; D000818:Animals; D005260:Female; D007073:Immunoglobulin E / Q000737:chemistry*; D051379:Mice; D008815:Mice, Inbred Strains; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000652:urine*; D011485:Protein Binding / Q000276:immunology; D011506:Proteins; D011852:Radioallergosorbent Test; D013379:Substrate Specificity
D000510:Alpha-Globulins; D011506:Proteins; C035737:major urinary proteins; D007073:Immunoglobulin E; D010447:Peptide Hydrolases; C023073:tosylarginine methyl ester hydrolase