Book ChapterDOI
The toxicological impact of some agents on glutathione S-transferase and cholinesterase enzymes
Fikret Türkan,Mehmet Nuri Atalar +1 more
- pp 281-290
TLDR
In this paper, the effects of avermectins, benzimidazole, antibiotics, and other groups of agents on glutathione S-transferase (GST), acetylcholinesterase (AChE), and butyrylcholine choline (BChE) enzymes were reviewed.Abstract:
In this chapter, we review the effects of some avermectins, benzimidazole, antibiotics, and other groups of agents on glutathione S-transferase (GST), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzymes. The enzyme inhibition of these compounds can be expressed as the toxicological effect. GST is one of the enzymes responsible for the elimination of toxic molecules, and AChE and BChE are important markers of Alzheimer's disease (AD) and both enzymes are identified as cholinesterases. Experimental studies on inhibition revealed that the used drugs have significant inhibitory effects on GST, BChE, and AChE enzymes. The agents with the best inhibition and toxicological effects were determined for each enzyme. In order to observe the inhibition studies, first IC50 values were followed and Ki studies were performed to observe the toxicological effect of each enzyme with these agents.read more
References
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Journal ArticleDOI
A new and rapid colorimetric determination of acetylcholinesterase activity.
TL;DR: A photometric method for determining acetylcholinesterase activity of tissue extracts, homogenates, cell suspensions, etc., has been described and Kinetic constants determined by this system for erythrocyte eholinesterases are presented.
Journal ArticleDOI
The role of glutathione-S-transferase in anti-cancer drug resistance
TL;DR: GSTs have emerged as a promising therapeutic target because specific isozymes are overexpressed in a wide variety of tumors and may play a role in the etiology of other diseases, including neurodegenerative diseases, multiple sclerosis, and asthma.
Journal ArticleDOI
Identification, characterization, and crystal structure of the Omega class glutathione transferases.
Philip G. Board,Marjorie Coggan,Gareth Chelvanayagam,Simon Easteal,Lars S. Jermiin,Gayle K. Schulte,Dennis E. Danley,Lise R. Hoth,Matthew C. Griffor,Ajith V. Kamath,Michele H. Rosner,Boris A. Chrunyk,David E. Perregaux,Christopher A. Gabel,Kieran F. Geoghegan,Jayvardhan Pandit +15 more
TL;DR: A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment, named Omega, which exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit.
Journal ArticleDOI
Theta, a new class of glutathione transferases purified from rat and man.
TL;DR: Glutathione transferases of a novel class, which it is proposed to term Theta, were purified from rat and human liver and partial analysis of primary structure shows that subunits 5, 12 and theta are related to each other.
Journal ArticleDOI
Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
Irmgard Sinning,Gerard J. Kleywegt,S. W. Cowan,Peter Reinemer,H.W. Dirr,Robert Huber,Gary L. Gilliland,Richard N. Armstrong,Xinhua Ji,Philip G. Board,B. Olin,Bengt Mannervik,T.A. Jones +12 more
TL;DR: The structure shows an overall similarity to the mu and pi class enzymes particularly in the glutathione-binding domain, but the main difference concerns the extended C terminus of the alpha class enzyme which forms an extra alpha-helix that blocks one entrance to the active site and makes up part of the substrate binding site.
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