Calorimetry of cholinesterase activity in serum.

Author:

O'Farrell H K,Chattopadhyay S K,Brown H D

Abstract

Abstract Cholinesterase activity in human serum was measured calorimetrically and compared to values obtained with the spectrophotometric method of Rappaport et al. [Clin. Chim. Acta 4, 227 (1959)]. The response of the calorimeter upon mixing serum with acetylcholine corresponded to the cholinesterase activity of the serum, the thermogram peak height being linearly related to enzyme activity at serum dilution volumes at which interference heat was negligible. The interference heat contributed by the dilution mixing characteristics of serum, studied separately, was found to be similar for heat-denatured, aged, or lyophilized samples. In all cases, heat of mixing was negligible when 1 ml of serum in buffer (2/3 by vol) was mixed with 1 ml of buffer. When this amount of serum was assayed with acetylcholine, cholinesterase activities of 2 and 3 kU/liter were recorded as thermograms with peak heights of 2.3 and 3.5 cm, respectively.

Publisher

Oxford University Press (OUP)

Subject

Biochemistry (medical),Clinical Biochemistry

Cited by 11 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Colorimetric detection of glucose and an assay for acetylcholinesterase with amine-terminated polydiacetylene vesicles;Chinese Science Bulletin;2011-05-18

2. History and New Developments of Assays for Cholinesterase Activity and Inhibition;Chemical Reviews;2010-07-01

3. Lactate Dehydrogenase Is an AU-rich Element-binding Protein That Directly Interacts with AUF1;Journal of Biological Chemistry;2002-09

4. Literaturverzeichnis;Analytische Methoden in der Biotechnologie;1991

5. Microcalorimetric determination of binding sites of acetylcholinesterase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1983-05

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