Immunological and Physicochemical Properties of a Highly Purified Allergen from Dirofilaria immitis
- 1 January 1979
- journal article
- research article
- Published by S. Karger AG in International Archives of Allergy and Immunology
- Vol. 60 (2), 121-131
- https://doi.org/10.1159/000232333
Abstract
Allergen in crude extract of Dirofilaria immitis was purified and separated from IgG-inducing antigens by a combination of DEAE-Sephadex A-50 chromatography, Sephadex G-200 gel filtration and starch gel zone electrophoresis. The purified preparation was proved to be one protein band by sodium dodecyl sulfate polyacrylamide gel (SDS-gel) electrophoresis and one precipitin arc by immunodiffusion. The molecular weight of the purified allergen was estimated to be approximately 20,000 by gel filtration and 15,000 by SDS-gel electrophoresis. The carbohydrate content of the preparation was apparently low, about 2%. The allergen was positively charged, and its determinant group was protein in nature. It was resistant to tryptic, pepsic and chymotryptic digestion, periodate oxidation and DNase and RNase digestion but very sensitive to pronase digestion. Allergen was inclined to aggregate each other in the buffered solution. It was also very resistant to vibration, heat (80°C for 1 h) and acid (pH 2.5) and alkali (pH 11.0) treatments. Rats as well as mice immunized with allergen developed only a reaginic antibody and no hemagglutination antibody.Keywords
This publication has 7 references indexed in Scilit:
- A sodium dodecyl sulfate micro-gel-electrophoresis technique suitable for routine laboratory analysisAnalytical Biochemistry, 1977
- A New Allergen from the Perienteric Fluid of Ascaris suum with Respect to ChargesInternational Archives of Allergy and Immunology, 1977
- Nucleotide Sequences in the Yeast Alanine Transfer Ribonucleic AcidJournal of Biological Chemistry, 1965
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- Periodate Oxidation of the Glycoprotein FetuinJournal of Biological Chemistry, 1964
- Isolation Studies of Allergens from Ragweed Pollen*Biochemistry, 1962
- The Chemistry of Allergens. VI. Chemical Composition and Properties of an Active Carbohydrate-free Protein from Cottonseed*,1Journal of the American Chemical Society, 1942