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二甲基亚砜在酶抑制研究中作为溶剂的应用:以醛糖还原酶为例。

The use of dimethylsulfoxide as a solvent in enzyme inhibition studies: the case of aldose reductase.

作者信息

Misuri Livia, Cappiello Mario, Balestri Francesco, Moschini Roberta, Barracco Vito, Mura Umberto, Del-Corso Antonella

机构信息

a Department of Biology, Biochemistry Unit , University of Pisa , Pisa , Italy.

b Tuscany Region PhD School in Biochemistry and Molecular Biology , Italy.

出版信息

J Enzyme Inhib Med Chem. 2017 Dec;32(1):1152-1158. doi: 10.1080/14756366.2017.1363744.

DOI:10.1080/14756366.2017.1363744
PMID:28856935
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6009938/
Abstract

Aldose reductase (AR) is an enzyme devoted to cell detoxification and at the same time is strongly involved in the aetiology of secondary diabetic complications and the amplification of inflammatory phenomena. AR is subjected to intense inhibition studies and dimethyl sulfoxide (DMSO) is often present in the assay mixture to keep the inhibitors in solution. DMSO was revealed to act as a weak but well detectable AR differential inhibitor, acting as a competitive inhibitor of the L-idose reduction, as a mixed type of non-competitive inhibitor of HNE reduction and being inactive towards 3-glutathionyl-4-hydroxynonanal transformation. A kinetic model of DMSO action with respect to differently acting inhibitors was analysed. Three AR inhibitors, namely the flavonoids neohesperidin dihydrochalcone, rutin and phloretin, were used to evaluate the effects of DMSO on the inhibition studies on the reduction of L-idose and HNE.

摘要

醛糖还原酶(AR)是一种致力于细胞解毒的酶,同时在继发性糖尿病并发症的病因学和炎症现象的放大中起重要作用。AR受到广泛的抑制研究,并且在测定混合物中经常存在二甲基亚砜(DMSO)以保持抑制剂溶解。已发现DMSO作为一种微弱但可检测到的AR差异抑制剂,作为L-艾杜糖还原的竞争性抑制剂,作为HNE还原的混合型非竞争性抑制剂,并且对3-谷胱甘肽基-4-羟基壬醛转化无活性。分析了DMSO对不同作用抑制剂的动力学作用模型。使用三种AR抑制剂,即类黄酮新橙皮苷二氢查耳酮、芦丁和根皮素,来评估DMSO对L-艾杜糖和HNE还原抑制研究的影响。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0e2/6009938/8a0c440da266/IENZ_A_1363744_F0004_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0e2/6009938/bf793177cdcb/IENZ_A_1363744_F0001_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0e2/6009938/57ecf241721d/IENZ_A_1363744_F0002_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0e2/6009938/34d3df8d921f/IENZ_A_1363744_F0003_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0e2/6009938/8a0c440da266/IENZ_A_1363744_F0004_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0e2/6009938/bf793177cdcb/IENZ_A_1363744_F0001_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0e2/6009938/57ecf241721d/IENZ_A_1363744_F0002_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0e2/6009938/34d3df8d921f/IENZ_A_1363744_F0003_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0e2/6009938/8a0c440da266/IENZ_A_1363744_F0004_B.jpg

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