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Environmental exposure to glyphosate does not inhibit human acetylcholinesterase and butyrylcholinesterase

Dora Kolić

Dora Kolić

Institute for Medical Research and Occupational Health, Division of ToxicologyZagreb, Croatia
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Kolić, Dora
, 
Vesna Pehar

Vesna Pehar

Dr Franjo Tuđman Croatian Defence AcademyZagreb, Croatia
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Pehar, Vesna
 et 
Zrinka Kovarik

Zrinka Kovarik

  • Institute for Medical Research and Occupational Health, Division of ToxicologyZagreb, Croatia
  • University of Zagreb Faculty of ScienceZagreb, Croatia
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Kovarik, Zrinka
  
29 mars 2024
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Catégorie d'article: Original article
Publié en ligne: 29 mars 2024
Pages: 76 - 80
Reçu: 01 janv. 2024
Accepté: 01 mars 2024
DOI: https://doi.org/10.2478/aiht-2024-75-3822
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© 2024 Dora Kolić et al., published by Sciendo
This work is licensed under the Creative Commons Attribution 4.0 International License.

Figure 1

Chemical structure of glyphosate
Chemical structure of glyphosate

Figure 2

Glyphosate inhibition profiles for human AChE and BChE shown as the dissociation constant of the enzyme-inhibitor complex (Ki, upper panels) and IC50 values (lower panels) determined in the presence of substrate acetylthiocholine (ATCh) over a range of glyphosate concentrations (c). The same dataset was used to determine both kinetic profiles. Inhibition was evaluated from four experiments measured at 25 °C
Glyphosate inhibition profiles for human AChE and BChE shown as the dissociation constant of the enzyme-inhibitor complex (Ki, upper panels) and IC50 values (lower panels) determined in the presence of substrate acetylthiocholine (ATCh) over a range of glyphosate concentrations (c). The same dataset was used to determine both kinetic profiles. Inhibition was evaluated from four experiments measured at 25 °C

Dissociation constants (Ki) of glyphosate for human AChE and BChE and approximated IC50 values

Enzyme Ki (mmol/L) Approx. IC50 (mmol/L)
AChE 28.4±2.7 25.1
BChE 19.3±1.8 20.0
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Médecine, Sciences médicales de base, Sciences médicales de base, autres
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