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dc.contributor.authorParham, Taslimi
dc.contributor.authorAfsun, Sujayev
dc.contributor.authorSevgi, Mamedova
dc.contributor.authorPinar, Kalin
dc.contributor.authorIlhami, Gulcin
dc.contributor.authorNastaran, Sadeghian
dc.contributor.authorSukru, Beydemir
dc.contributor.authorO. Irfan, Kufrevioglu
dc.contributor.authorSaleh H., Alwasel
dc.contributor.authorVagif, Farzaliyev
dc.contributor.authorSabir, Mamedov
dc.date.accessioned2019-05-17T06:51:29Z
dc.date.available2019-05-17T06:51:29Z
dc.date.issued2017
dc.identifier.urihttp://hdl.handle.net/11772/1187
dc.description.abstract1-(4-Methylsulfonyl)-2-thione-4-aryl-5-Z-6-methyl and oxyalkyl-imidazoles were synthesized from different tetrahydropyrimidinethiones and aryl sulfonyl chloride. These compunds were tested for metal chelating effects and to determine the phrase in which inhibition occured between two physiologically pertinent compunds and carbonic anhydrase (CA) isozymes I and II (hCA I and II), butyrylcholinesterase (BChE) and acetylcholinesterase (AChE). AChE was detected in high concentrations in the brain and red blood cells. BChE is another enzymes that is abundant available in the liver and released into the blood in a soluble form. Newly synthesized hetaryl sulfonamides exhibited impressive inhibition profiles with Ki values in the range of 1.42-6.58 nM against hCA I, 1.72-7.41 nM against hCA II, 0.20-1.14 nM against AChE and 1.55-5.92 nM against BChE. Moreover, acetazolamide showed Ki values of 43.69 +/- 6.44 nM against hCA I and 31.67 +/- 8.39 nM against hCA II. Additionally, tacrine showed Ki values of 25.75 +/- 3.39 nM and 37.82 +/- 2.08 against AChE and BChE, respectively.en_US
dc.language.isoengen_US
dc.publisherInformaen_US
dc.relation.isversionof10.1080/14756366.2016.1238367en_US
dc.rightsinfo:eu-repo/semantics/restrictedAccessen_US
dc.subjectAcetylcholinesteraseen_US
dc.subjectAryl sulfonyl chloridesen_US
dc.subjectButyrylcholinesteraseen_US
dc.subjectCarbonic anhydraseen_US
dc.subjectHeterocyclic aminesen_US
dc.titleSynthesis and bioactivity of several new hetaryl sulfonamidesen_US
dc.typearticleen_US
dc.relation.journalJournal of Enzyme Inhibition and Medicinal Chemistryen_US
dc.contributor.departmentBartın Üniversitesi, Fen Fakültesi, Biyoteknoloji Bölümüen_US
dc.identifier.volume32en_US
dc.identifier.issue1en_US
dc.identifier.startpage137en_US
dc.identifier.endpage145en_US


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