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Cysteinyl Proteinases of Schistosoma mansoni Eggs: Purification and Partial Characterization

Chin K. Sung and Marc H. Dresden
The Journal of Parasitology
Vol. 72, No. 6 (Dec., 1986), pp. 891-900
DOI: 10.2307/3281841
Stable URL: http://www.jstor.org/stable/3281841
Page Count: 10
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Cysteinyl Proteinases of Schistosoma mansoni Eggs: Purification and Partial Characterization
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Abstract

The egg stage of Schistosoma mansoni, a trematode blood fluke, is known to be responsible for an immunologically mediated granuloma formation. Proteolytic enzymes of S. mansoni eggs may be involved in the penetration of host tissue by eggs and/or may act as antigens to cause a humoral as well as a cell-mediated response leading to granuloma formation. Three acidic, thiol-dependent proteinases from the eggs of S. mansoni were isolated, and 2 major proteinases (I and II) were purified to homogeneity using chromatofocusing, AcA54 ultrogel chromatography, and thiopropyl-Sepharose 6B affinity chromatography. Proteinases I and II have molecular weights of 25,400 and 30,500, and isoelectric points of 6.0 and 5.6, respectively. These enzymes were found to be cathespin B-like cysteinyl proteinases based on similarities in molecular weight, isoelectric point, optimal assay pH, instability to neutral pH, substrate specificity, and inhibitor sensitivity. A monoclonal antibody, specific to S. mansoni egg proteinases was used in immunoblotting studies. Under native, but not under denaturing, conditions for gel electrophoresis, this monoclonal antibody reacted with egg proteinases. This antibody had previously been shown to recognize an antigen in the miracidial penetration glands of schistosome eggs.

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