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An initial characterization of the proteolytic enzymes secreted by the adult stage of the human hookworm Necator americanus

Published online by Cambridge University Press:  06 April 2009

A. Brown ,
J. M. Burleigh ,
E. E. Billett  and
D. I. Pritchard
A. Brown
Affiliation:
Department of Life Sciences, Nottingham Trent University, Nottingham NG11 8NS
J. M. Burleigh
Affiliation:
Department of Life Sciences, Nottingham Trent University, Nottingham NG11 8NS
E. E. Billett
Affiliation:
Department of Life Sciences, Nottingham Trent University, Nottingham NG11 8NS
D. I. Pritchard
Affiliation:
Department of Life Science, University of Nottingham, Nottingham NG7 2RD
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Summary

The proteolytic activities present in adult Necator americanus excretory–secretory products have been assessed using biologically relevant, naturally occurring substrates (haemoglobin and fibrinogen) and a number of synthetic fluorogenic and chromogenic substrates. One broad peak of activity was observed against haemoglobin in the pH range 5 to 7, with maximum activity at pH 6·6, while fibrinogenolytic activity was shown to be greater at pH 3·5. Inhibition studies against haemoglobin, fibrinogen and synthetic substrates using a battery of appropriate protease inhibitors indicated the presence of a mixture of aspartyl, cysteinyl and serine proteases. Metal ion (Ca2+, Zn2+ and Fe2+) stimulation was demonstrated, with stimulation by Zn2+ being the most marked. These results are discussed in the context of recent developments in the field of parasite proteolytic enzymes, where they have been suggested as targets for immuno- and chemotherapy.

Keywords

Necator americanusproteolytic enzymeshaemoglobinase
Type
Research Article
Information
Parasitology , Volume 110 , Issue 5 , June 1995 , pp. 555 - 563
Copyright
Copyright © Cambridge University Press 1995

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