Isolation and Partial Characterization of the Allergen in Mountain Cedar Pollen

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Abstract
A biologically active fraction from a crude extract of mountain cedar pollen was purified and partially chemically characterized. An ammonium bicarbonate extract of commercial defatted pollen was fractionated by G-100 Sephadex chromatography and the biologically active fraction was homogeneous by polyacrylamide gel electrophoresis and N-terminal amino acid sequence analysis. The biologically active component is a 50,000 dalton protein whose N-terminal amino acid sequence is Asp-Asn-Pro-Ile-Asp. These findings provide a further purified pollen allergen for immunologic studies and the 1st such purified allergen having clinical significance in a limited geographic region.