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Monoamine oxidase in adult Hymenolepis diminuta (Cestoda)

Published online by Cambridge University Press:  06 April 2009

M. Sanchez Moreno  and
J. Barrett
M. Sanchez Moreno
Affiliation:
Department of Zoology, University College of Wales, Aberystwyth, Dyfed, SY23 3DA
J. Barrett
Affiliation:
Department of Zoology, University College of Wales, Aberystwyth, Dyfed, SY23 3DA
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Summary

A membrane-bound monoamine oxidase (EC 1.4.3.4) was demonstrated in homogenates of Hymenolepis diminuta. The enzyme oxidized a variety of biologically active amines (in decreasing order: dopamine, adrenaline, noradrenaline, tryptamine, tyramine, octopamine), there was, however, no activity with 5-hydroxytryptamine or benzylamine. No diamine oxidase (EC 1.4.3.6) could be detected in H. diminuta (using histamine, cadaverine or putrescine as substrates). The monoamine oxidase from H. diminuta was not inhibited by azide, hydroxylamine or semicarbazide, but was inhibited by cupferron, α-α dipyridyl and iodoacetamide, and by the specific monoamine oxidase inhibitors pargyline, nialamide and iproniazid. Several anthelmintics were also found to be inhibitors of monoamine oxidase. The possible roles of monoamine oxidase in H. diminuta are discussed.

Type
Research Article
Information
Parasitology , Volume 78 , Issue 1 , February 1979 , pp. 1 - 5
Copyright
Copyright © Cambridge University Press 1979

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References

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