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Further Purification and Characterization of a Circulating Antigen in Schistosomiasis

From the Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20014 and the Laboratory for Carbohydrate Research, Department of Biological Chemistry and Medicine, Harvard Medical School and Massachusetts General Hospital, Boston, Massachusetts 02114

Abstract

Previous studies showed that an antigen found in the circulation of animals heavily infected with Schistosoma mansoni was extracted in a trichloroacetic acid solublechloroform insoluble fraction (TCA-S-C) of adult worms. Antigenic activity was destroyed by periodate treatment but remained unaltered after treatment with proteolytic enzymes, DNase, RNase, and lyophilization. In the present study, chromatography of TCA-S-C on a DEAE cellulose column revealed six substances, one of which was antigenic. After electrophoresis in agarose antigenic activity corresponded to a slower moving, toluidine blue-staining material. A faster moving, toluidine blue-staining substance seems to be responsible for the large 260 nm. absorbing peak. Analysis of a fraction containing only antigen revealed a large amount of carbohydrate, primarily N-acetylglucosamine and D-glucuronic acid but also galactase, glucose, N-acetylglucosamine, and trace amounts of other sugars. Amino acids accounted for about 11% of the weight of the antigen. The antigen appears to be a proteoglycan.

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				A. v. Remoortere, C. H.Hokke, G. J.v. Dam, I. v. Die, A. M.Deelder, and D. H.v. d. Eijnden Various stages of Schistosoma express Lewisx, LacdiNAc, GalNAc{beta}1-4 (Fuc{alpha}1-3)GlcNAc and GalNAc{beta}1-4(Fuc{alpha}1-2Fuc{alpha}1-3)GlcNAc carbohydrate epitopes: detection with monoclonal antibodies that are characterized by enzymatically synthesized neoglycoproteins Glycobiology, June 1, 2000; 10(6): 601 - 609. [Abstract] [Full Text] [PDF]