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The activity of acid proteases hydrolysing haemoglobin in parasitic helminths with special reference to interspecific and intraspecific distribution

Published online by Cambridge University Press:  06 April 2009

Jun Maki ,
Asami Furuhashi  and
Toshio Yanagisawa
Jun Maki
Affiliation:
Department of Parasitology, Kitasato University School of Medicine, Sagamihara 228, Kanagawa, Japan
Asami Furuhashi
Affiliation:
Department of Parasitology, Kitasato University School of Medicine, Sagamihara 228, Kanagawa, Japan
Toshio Yanagisawa
Affiliation:
Department of Parasitology, Kitasato University School of Medicine, Sagamihara 228, Kanagawa, Japan
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Summary

Acid proteases hydrolysing haemoglobin, first described by Timms & Bueding (1959), were studied to investigate the interspecific and intraspecific distribution in adult parasitic helminths. Acid protease activity was detected in a variety of adult helminths, irrespective of their habitats, namely, parasitic nematodes, Angiostrongylus cantonensis, Dirofilaria immitis, Trichuris muris and Ascaris suum, a trematode, Paramphistomum sp. and cestodes, Diphyllobothrium erinacei and Hymenolepis nana. Much higher specific activity was observed in the blood nematodes, A. cantonensis and D. immitis than in the gastro-intestinal helminths examined. The intraspecific distribution of the acid protease activity within organs was studied in those nematodes from which the organs could be anatomically separated. The highest specific activity was observed in the intestine of A. cantonensis, D. immitis and A. suum. The activity was also found in other organs of these nematodes, namely, the reproductive organs and the body wall, but to a much lesser extent. The pH optima for the hydrolysis of haemoglobin were found to be in the pH range of 3·1 to 4·6. Each of the enzyme solutions from the 7 species of helminths hydrolysed haemoglobin faster than the other proteins examined but some activity on myoglobin, casein, albumin and other proteins was demonstrated. Pepstatin, a potent inhibitor of carboxyl proteases, inhibited the hydrolysis of haemoglobin by the acid proteases of the 7 species of the parasites. Acid protease activity from A. cantonensis and A. suum was not inhibited in the presence of thiol-, serine- and metallo-protease inhibitors at a concentration of 10−6 M. This fact, together with the inhibitory effect of pepstatin, suggests that the enzyme activity is likely to be due to carboxyl protease(s). Acid proteases such as cathepsin D and pepsin were simultaneously used for comparison of some enzymological characteristics. The substrate specificity of the enzyme solutions from the helminths seemed to resemble that of cathepsin D rather than that of pepsin. The effects of pH and pepstatin on the acid protease activity of the helminths were similar to those on pepsin and cathepsin D.

Type
Research Article
Information
Parasitology , Volume 84 , Issue 1 , February 1982 , pp. 137 - 147
Copyright
Copyright © Cambridge University Press 1982

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