ESTERASE FROM AMMONIATED LATEX - BIOCHEMICAL-CHARACTERIZATION AND ANTIGENICITY

Latex allergy is a recently increasing hazard to people who are repeat edly in contact with Latex products. Notably, with this allergy, cross -reactivity to vegetable foods and pollen is frequently observed. It i s postulated that pathogenesis- or, rather, defence-related proteins i nduced in rubber trees are responsible for the Latex allergy and the c ross-reactivity. To evaluate this hypothesis, an esterase was selected as one of the probable defence-related proteins in rubber Latex and i ts involvement in Latex allergy was investigated. The biochemical prop erties of a chromatographically purified esterase from ammoniated Late x were compared with those of esterases (hevains) previously purified from rubber Latex. The antigenicity of the esterase was examined by im munoblotting using sera from Latex-allergic patients. The purified est erase (of molecular weight 80 kDa) dissociated into subunits under den aturing conditions and shared biochemical properties with hevain 1 fro m lutoids. The esterase was recognized by IgE in patients' sera. This suggests the relevance of the purified esterase to Latex allergy.