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Journal ArticleDOI

A new approach to determining cholinesterase activities in samples of whole blood.

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TLDR
A sensitive method, especially suitable for clinical laboratories, for the routine determination of cholinesterase activities in whole blood is presented, based on the hydrolysis of propionylthiocholine and the spectrophotometric determination of the thiocholine produced by reaction with 4,4'-dithiodipyridine.
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This article is published in Clinica Chimica Acta.The article was published on 1978-10-16. It has received 114 citations till now. The article focuses on the topics: Whole blood & Cholinesterase.

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Citations
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Journal ArticleDOI

Improved determination of acetylcholinesterase activity in human whole blood.

TL;DR: This modified approach provides a simple way for sensitive and precise determination of AChE activity in whole blood in the presence of organophosphates even with low-tech equipment.
Journal ArticleDOI

Dried blood spots in toxicology: from the cradle to the grave?

TL;DR: This review provides a comprehensive overview of the distinct subdisciplines of toxicology for which DBS sampling has been applied, and discusses the strengths and limitations of DBS in the different subdiscipline and provides future prospects for the use of this promising sampling technique in toxicology.
Journal ArticleDOI

Muscarinic receptors in human SH-SY5Y neuroblastoma cell line: regulation by phorbol ester and retinoic acid-induced differentiation ☆

TL;DR: It is demonstrated that TPA and RA can regulate both the number of muscarinic receptors and the acetylcholinesterase activity in human SH-SY5Y neuroblastoma cells.
Journal ArticleDOI

Cholinesterase status, pharmacokinetics and laboratory findings during obidoxime therapy in organophosphate poisoned patients:

TL;DR: Signs of transiently impaired liver function were observed in patients who showed transient multi- organ failure, and it is advisable to keep the plasma concentration of obidoxime at 10 - 20 μM, although the full reactivating potential of obdoxime will not then be exploited.
Journal Article

The anticancer prodrug CPT-11 is a potent inhibitor of acetylcholinesterase but is rapidly catalyzed to SN-38 by butyrylcholinesterase.

TL;DR: Modeling of CPT-11 within the predicted active site of AcChE and BuChE corroborated experimental results indicating that, although the drug was oriented correctly for activation, the constraints dictated by the active site gorge were such that C PT-11 would be unlikely to be activated by AcE.
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

Determination of sulfhydryl groups with 2,2′- or 4,4′-dithiodipyridine☆

TL;DR: The proposed method is compared with known methods for the determination of sulfhydryl groups and permits determination of SH groups in simple compounds and in biological materials.
Journal ArticleDOI

A method for the detection of atypical forms of human serum cholinesterase. determination of dibucaine numbers

TL;DR: Cases with atypical ester enzyme activity were found by determining esterase inhibition in numerous sera using the local anaesthetic dibucaine (cinchocaine, TN Nupercaine, Perkain), and the degree of inhibition measured under these conditions and expressed in per cent has been termed "Dibucain Number".
Journal ArticleDOI

Red cell and plasma cholinesterase activities in microsamples of human and animal blood determined simultaneously by a modified acetylthiocholine-DTNB procedure.

TL;DR: A modification of the DTNB method was developed for the simultaneous determination of red cell and plasma cholinesterases in samples of only 0.01-0.03 ml of whole human and animal blood, using a relatively short incubation period of 10 min and an incubation temperature of 30°C as mentioned in this paper.
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