Schistosoma mansoni: thiol proteinase properties of adult worm "hemoglobinase". |
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Authors: | M H Dresden A M Deelder |
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Institution: | 1. Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030, U.S.A.;2. Laboratory of Parasitology, University of Leiden, Leiden, The Netherlands |
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Abstract: | This report presents evidence that the “hemoglobinase” from adult Schistosoma mansoni, first described by Timms and Bueding and later by Senft and his collaborators, belongs to the class of thiol proteinases. Proteolytic activity is stimulated by SH-containing compounds and inhibited by N-ethylmaleimide as well as other inhibitors of thiol proteinases. The enzyme can be partially purified by affinity chromatography using a Sepharose-linked organomercurial ligand. In addition to its activity on globin and hemoglobin, the enzyme can also be assayed with Azocoll, a general protease substrate, and by the activation of inactive trypsinogen to active trypsin. Extraction of the enzyme is enhanced by the addition of the nonionic detergent Triton X-100. |
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Keywords: | Trematode Proteinases Proteinase inhibitors Thiols Azocoll Affinity chromatography Trypsinogen activation Triton X-100 Hamster golden |
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