IGE-BINDING TRYPSIN-INHIBITORS IN PLANT POLLEN EXTRACTS

In an attempt to access the possible role of protease-antiprotease mec hanisms of non-immune defence in pollinosis, only low levels of trypsi n-, kallikrein- or plasmin-like proteinases could be detected in aqueo us pollen extracts. In contrast, several pollen species displayed appr eciable trypsin inhibitory activity, e.g. Parietaria, Olea, Ambrosia, Rumex, Chenopodium, Holcus and Poa spp. These proteins of the serpin f amily of anti-proteinases were found to bind specific IgE-antibodies f rom the serum of hay fever patients. As examples, the IgE-binding tryp sin inhibitors from the pollen of Parietaria judaica and Ambrosia elat ior were purified and characterized as acidic proteins with pI 4.2 and a molecular weight of 20-24 kDa.