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Chemosensory Mechanism in American Cockroach Olfaction and Gustation
ALTHOUGH numerous theories of olfaction and gustation 1–8 have been published, there is little experimental evidence on the energy-transfer mechanisms involved in the interactions of chemical messengers with proteinaceous receptors of sensory neurones. One such mechanism, involved in the inhibition...
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Published in: | Nature (London) 1973-08, Vol.244 (5415), p.370-371 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | ALTHOUGH numerous theories of olfaction and gustation
1–8
have been published, there is little experimental evidence on the energy-transfer mechanisms involved in the interactions of chemical messengers with proteinaceous receptors of sensory neurones. One such mechanism, involved in the inhibition of feeding of
Periplaneta americana
and
Scolytus multistriatus
by various 1,4-naphthoquinones, has been extensively studied and partially interpreted behaviourally
9–16
, ultrastructurally
10–16
, electrophysiologically
10–16
and biochemically
10–16
. These messenger naphthoquinones were shown to act through a selective reaction with sulphydryl
10–16
groups in a particular membrane-associated receptor macromolecule which was proven to be physically accessible
in situ
17
to these chemicals through cuticular pores and tubules
10–16
in the walls of chemoreceptor sensillae on the insect's antennae. This specific energy transfer resulted in disulphide-bond formation or thiol complexing
10–16
, both of which are proven
18
mechanisms in certain proteins for causing conformational changes. Such changes can alter the cationic permeability of macromolecules composing membranes
18
. The messenger-altered cation permeability of the receptor thus can result in the generation of action potentials in the sensory neurone
10–16
. Here we report certain physicochemical characteristics of the messenger-naphthoquinone receptor protein interactions as analysed in a deoxygenated system at physiological
p
H by the
in vitro
technique of dropping mercury electrode (DME) polarography (PO4 ‘Polariter’, London Co.). The polarogram is a current–voltage curve obtained by applying a gradually increasing voltage to a system and measuring the current flow at each potential. Characteristic polarographic half-wave potential (that is, E ½) values for proteins were attributed exclusively to exposed, reactive sulphydry
1
, or reducible disulphide, groups
19–22
. In our own investigations, the ‘Triton’ X-100-solubilized quinone-reactive receptor protein from the cockroach antennae gave a characteristic E ½ of −1,860 mV. A control (non-quinone receptor) protein system composed of the saline-soluble proteins from the same antennae gave an E ½ of −1,800 mV. Adding messenger 5-hydroxy-1,4-naphthoquinone (5 × 10
−5
M) in the receptor preparation characteristically shifted the E ½ from −1,860 to −1,880 mV; another less repellent, or feeding-inhibitory, messenger, 2-methyl-1,4-naphthoquinone (5 × 10
−5
M), |
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ISSN: | 0028-0836 1476-4687 |
DOI: | 10.1038/244370a0 |