IgE-mediated hypersensitivity to proteins eluting from surgical gloves and other natural rubber products is a well-recognized allergic condition with special impact to health care workers and sensitized patients. Since rubber elongation factor (REF) has been suggested to be the major latex allergen (Hev b 1) we purified REF from rubber particles using electrophoresis and electroelution and reevaluated the occurrence of IgE antibodies to purified REF. The purified protein was subjected to tryptic digestion, peptide separation and amino acid sequencing. Amino acid sequences of 9 tryptic peptides from the purified 14-kD protein gave 100 homology to REF. In immunoblotting, sera from 4 of 6 latex-allergic children with spina bifida or other congenital anomalies exhibited IgE antibodies against REF whereas only 1 serum from the 30 other latex-allergic patients had similar antibodies. In IgE ELISA 8/45 (18) latex-allergic patients had IgE antibodies to purified REF, whereas 30 (67) of the same patients had IgE antibodies to purified prohevein, another rubber protein, recently shown to be a major natural rubber latex allergen. The observed overall low frequency of IgE antibodies to purified REF, as measured by two specific IgE assays, indicates that REF is one but not the most significant allergen among the natural rubber latex proteins.
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