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Demonstration of carboxyl and thiol protease activities in adult Schistosoma mansoni, Dirofilaria immitis, Angiostrongylus cantonensis and Ascaris suum

Published online by Cambridge University Press:  18 November 2009

Jun Maki  and
Toshio Yanagisawa
Jun Maki
Affiliation:
Department of Parasitology, Kitasato University School of Medicine, Sagamihara, Kanagawa, 228 Japan.
Toshio Yanagisawa
Affiliation:
Department of Parasitology, Kitasato University School of Medicine, Sagamihara, Kanagawa, 228 Japan.
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Abstract

Evidence has been presented showing two kinds of acidic protease activities in adult Schistosoma mansoni, Dirofilaria immitis, Angiostrongylus cantonensis and Ascaris suum. A haemoglobinolytic activity without adding any SH-containing compounds was maximal at pH 3.5, 2.5, 30 and 3.5 in S. mansoni, D. immitis, Angiostrongylus cantonensis and Ascaris suum respectively. The inhibitor studies demonstrated that this activity is ascribable to carboxyl protease(s). In the presence of dithiothreitol, activity on Azocoll (azo-dye coupled hide powder) was maximal at pH 4.6, 4.6, 3.5 and 5.6 in S. mansoni, D. immitis, Angiostrongylus cantonensis and Ascaris suum respectively. The effects of inhibitors demonstrated that this activity belongs to the thiol protease class. The intraspecific distribution of the protease activities was studied in some of the nematodes from which the organs could be anatomically separated. The distribution patterns of the haemoglobinolytic and azocollytic activities were quite different in An. cantonensis and much the same in As. suum. Based on the present results, acidic haemoglobinolytic activities reported in adult S. mansoni by other authors are thought to be due to carboxyl and thiol protease(s) respectively.

Keywords

Schistosoma mansoniDirofilaria immitisAscaris suumAngiostrongylus cantonensisthiol proteasescarboxyl proteases
Type
Research Papers
Information
Journal of Helminthology , Volume 60 , Issue 1 , March 1986 , pp. 31 - 37
Copyright
Copyright © Cambridge University Press 1986

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