Separation and characterization of hydrophilic and detergent-interacting components of brain acetylcholinesterase from Tenebrio molitor L. (insecta, coleoptera)

Lenoir-Rousseaux, Jean-Jacques; Arpagaus, Martine; Toutant, Jean‐Pierre

doi:10.1016/0305-0491(88)90033-8

Cited by 4 publications

(5 citation statements)

References 22 publications

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“…Much evidence tends to show that insect AChE may exist in hydrophilic and amphiphilic (membrane-bound) states. So far, this has been reported for Coleoptera [16], Lepidoptera [17,18] and Diptera [15,19], and the proportions of both states vary from species to species. Studies carried out in the present work, especially by use of the Triton X-1 14 phase-separation method, confirm that this is also the case in a Hymenopteran species.…”

Section: Discussionmentioning

confidence: 79%

“…Some authors have described the existence of a single membrane AChE whose apparent sedimentation coefficient varies from 5.4S to 5.7 S [9-11], whereas others have shown the presence of distinct biochemical variants [6,[12][13][14]. Recent studies carried out in Drosophila melanogaster [15], Tenebrio molitor [16], Pieris brassicae [17,18] and on purified AChE from the housefly Musca domestica [19] have allowed the characterization of globular membrane forms with their hydrophilic counterparts.…”

Section: Introductionmentioning

confidence: 99%

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Acetylcholinesterase from Apis mellifera head. Evidence for amphiphilic and hydrophilic forms characterized by Triton X-114 phase separation

Belzunces¹,

Toutant²,

Bounias³

1988

Biochemical Journal

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The polymorphism of bee acetylcholinesterase was studied by sucrose-gradient-sedimentation analysis and non-denaturing electrophoretic analysis of fresh extracts. Lubrol-containing extracts exhibited only one form, which sedimented at 5 S when analysed on high-salt Lubrol-containing gradients and 6 S when analysed on low-salt Lubrol-containing gradients. The 5 S/6 S form aggregated upon removal of the detergent when sedimented on detergent-free gradients and was recovered in the detergent phase after Triton X-114 phase separation. Thus the 5 S/6 S enzyme corresponds to an amphiphilic acetylcholinesterase form. In detergent-free extracts three forms, whose apparent sedimentation coefficients are 14 S, 11 S and 7 S, were observed when sedimentations were performed on detergent-free gradients. Sedimentation analyses on detergent-containing gradients showed only a 5 S peak in high-salt detergent-free extracts and a 6 S peak, with a shoulder at about 7 S, in low-salt detergent-free extracts. Electrophoretic analysis in the presence of detergent demonstrated that the 14 S and 11 S peaks corresponded to aggregates of the 5 S/6 S form, whereas the 7 S peak corresponded to a hydrophilic acetylcholinesterase form which was recovered in the aqueous phase following Triton X-114 phase separation. The 5 S/6 S amphiphilic form could be converted into a 7.1 S hydrophilic form by phosphatidylinositol-specific phospholipase C digestion.

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Section: Discussionmentioning

confidence: 79%

Section: Introductionmentioning

confidence: 99%

Acetylcholinesterase from Apis mellifera head. Evidence for amphiphilic and hydrophilic forms characterized by Triton X-114 phase separation

Belzunces¹,

Toutant²,

Bounias³

1988

Biochemical Journal

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“…Biochemical and pharmacological properties of AChE have been characterized in many insect species (Devonshire, 1975;Devonshire and Moores, 1994a,b;Brestkin et al, 1985Brestkin et al, , 1992Lester and Gilbert, 1987;Gnagey et al, 1987;Lenoir-Rousseaux and Gautron, 1987;Lenoir-Rousseaux et al, 1988;Brown and Bryson, 1992;Zhu and Brindley, 1992a-d;Argentine et al, 1994;Clark, 1994, 1995;Xu and Bull, 1994a,b;Pandey and Sharma, 1996;Guedes et al, 1998). Numerous studies have shown several typical features of insect AChE, including:…”

Section: Introductionmentioning

confidence: 95%

Purification and kinetic analysis of acetylcholinesterase from western corn rootworm,Diabrotica virgifera virgifera (Coleoptera: Chrysomelidae)

Gao

Rao

Wilde

et al. 1998

Arch. Insect Biochem. Physiol.

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“…This classification only describes the quaternary structure of the molecules and does not take into account their interaction with detergents. The existence or the absence of a direct interaction of AChE with non-denaturing detergent is now used to characterize amphiphilic and hydrophilic forms of AChE from most species: one class does not bind detergent and is hydrophilic, the second class interacts with detergents and for this reason is called hydrophobic or amphiphilic (Fournier et al 1987, Lenoir-Rousseaux et al 1988.…”

Section: Inhibitory Effects Of Organophosphorous and Carbamate Mixturmentioning

confidence: 99%

Joint action of combinations of pollutants on the acetylcholinesterase activity of several marine species

Bocquené

Bellanger²,

Cadiou³

et al. 1995

Ecotoxicology

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: Acetylcholinesterase (AChE) is used as a specific biomarker of the effects of organophosphorous (OP) and carbamate (C) insecticides on the coastal marine environment. Studies of mixtures (by pairs) of five of these substances showed cumulative, synergistic inhibitory effects in all cases. The strongest synergy was observed in organophosphate-carbamate mixtures (OP-C) and the least in mixtures of substances of the same type (OP-OP, C-C). The intensity of the synergistic effect was directly related to the length of time the enzyme was incubated with the inhibitory mixtures. Among the major organic contaminants of the marine environment, DDT and lindane (organochlorines), as well as atrazine and isoproturon, are not AChE inhibitors and had no effect on the inhibitory action of the OP and C insecticides tested. Among contaminants of metallic origin, zinc chloride, cadmium chloride, tributyltin chloride and methylmercury did not inhibit AChE at the concentrations measured in the different marine compartments (water, sediment, living matter). Mercuric chloride and arsenite had a weak inhibitory action in certain organisms. Zinc chloride, cadmium chloride and arsenic enhanced the inhibitory effects of some OP and C insecticides. The dragonet (Callionymus lyra) proved to be a particularly sensitive target species for monitoring pollutant effects.

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Separation and characterization of hydrophilic and detergent-interacting components of brain acetylcholinesterase from Tenebrio molitor L. (insecta, coleoptera)

Cited by 4 publications

References 22 publications

Acetylcholinesterase from Apis mellifera head. Evidence for amphiphilic and hydrophilic forms characterized by Triton X-114 phase separation

Acetylcholinesterase from Apis mellifera head. Evidence for amphiphilic and hydrophilic forms characterized by Triton X-114 phase separation

Purification and kinetic analysis of acetylcholinesterase from western corn rootworm,Diabrotica virgifera virgifera (Coleoptera: Chrysomelidae)

Joint action of combinations of pollutants on the acetylcholinesterase activity of several marine species

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