PURIFICATION AND PARTIAL AMINO-ACID SEQUENCING OF A 27-KD NATURAL-RUBBER ALLERGEN RECOGNIZED BY LATEX-ALLERGIC CHILDREN WITH SPINA-BIFIDA

We purified from natural rubber latex (NRL) by means of high-performan ce liquid chromatography a 27-kD protein, recognized characteristicall y by IgE in sera from latex-allergic children with spina bifida or oth er congenital anomalies and histories of multiple surgeries. N-termina l sequence analysis of the purified 27-kD protein was unsuccessful sug gesting that its N-terminus is blocked. To obtain internal sequence in formation from the protein it was digested with trypsin and the purifi ed tryptic peptides were subjected to sequence analysis. Thirteen of t he 14 sequenced peptides revealed no significant homology to any of th e published protein sequences indicating that the 27-kD protein is pre viously undescribed at the primary structure level. However, one of th e 14 sequenced peptides showed significant homology to the rubber elon gation factor, a 14.6-kD NRL protein. For the time being, the 27-kD NR L protein is the first molecularly characterized NRL allergen associat ed with defined clinical manifestations of latex allergy.