Isolation and partial characterization of the allergen in mountain cedar pollen.
A biologically active fraction from a crude extract of mountain cedar pollen has been 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 found to be 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 first such purified allergen having clinical significance in a limited geographic region.
D000485:Allergens / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D011058:Pollen / Q000032:analysis*; D012882:Skin Tests; D014197:Trees
D000485:Allergens