Ultraviolet spectrophotometric method for determination of cholinesterase activity with acetylcholine as a substrate.

Journal of applied biochemistry Pub Date : 1985-08-01
K Tomita, S Kamei, T Shiraishi, Y Hashimoto, M Yamanaka
{"title":"Ultraviolet spectrophotometric method for determination of cholinesterase activity with acetylcholine as a substrate.","authors":"K Tomita,&nbsp;S Kamei,&nbsp;T Shiraishi,&nbsp;Y Hashimoto,&nbsp;M Yamanaka","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>An enzymatic method for the determination of serum cholinesterase (ChE) activity is described. The method is based on the liberation of acetate from acetylcholine as a substrate by ChE and the conversion of the acetate to acetylphosphate and ADP in the presence of ATP by acetate kinase. The produced ADP is coupled with pyruvate kinase and lactate dehydrogenase in the presence of phosphoenolpyruvate and NADH. The amount of NADH consumed is determined by absorbance at 340 nm. The reaction proceeds stoichiometrically, and the dilution curve is linear up to 3300 U/liter. The results obtained by this method show a good correlation with those obtained by the usual methods.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1985-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of applied biochemistry","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

An enzymatic method for the determination of serum cholinesterase (ChE) activity is described. The method is based on the liberation of acetate from acetylcholine as a substrate by ChE and the conversion of the acetate to acetylphosphate and ADP in the presence of ATP by acetate kinase. The produced ADP is coupled with pyruvate kinase and lactate dehydrogenase in the presence of phosphoenolpyruvate and NADH. The amount of NADH consumed is determined by absorbance at 340 nm. The reaction proceeds stoichiometrically, and the dilution curve is linear up to 3300 U/liter. The results obtained by this method show a good correlation with those obtained by the usual methods.

分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
以乙酰胆碱为底物的紫外分光光度法测定胆碱酯酶活性。
描述了一种测定血清胆碱酯酶(ChE)活性的酶法。该方法是基于乙酰胆碱作为底物通过ChE将乙酸酯从乙酰胆碱中解放出来,并在ATP存在下通过乙酸激酶将乙酸酯转化为乙酰磷酸和ADP。产生的ADP在磷酸烯醇丙酮酸和NADH存在下与丙酮酸激酶和乳酸脱氢酶偶联。NADH的消耗量由340 nm处的吸光度测定。反应进行化学计量,稀释曲线线性上升到3300 U/l。该方法得到的结果与常用方法得到的结果具有良好的相关性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Influence of angiotensin-converting enzyme inhibitor, foroxymithine, on dynamic equilibrium around the renin-angiotensin system in vivo. Assessment of internal primary structure of polypeptides newly translated in vitro by reticulocyte lysate: a study with cytochrome b5. Immunosorbent consisting of DNA immobilized on oxirane-activated sepharose. Syntheses and effects of a thymopoietin II fragment and its analogs on the impaired T-cell transformation in a patient with common variable immunodeficiency. Simplified separation of myosin from rabbit liver.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1