volume 82, issue 5, P818-827 1988
DOI: 10.1016/0091-6749(88)90084-x
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Abstract: Commercial Solenopsis invicta (Sol i) venom was fractionated by gel filtration and high-performance cation exchange chromatography. Four proteins were isolated and purified to homogeneity. The four proteins were tested with a panel of sera from patients allergic to fire ant venom; all proteins had significant allergenic activity. These proteins corresponded to four of the bands we previously reported to be allergenic by immunoblot analysis. Sol i I has an apparent molecular weight of 37,000 daltons and yields …

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