Synephrine and phenylephrine act as -amylase, -glycosidase, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase enzymes inhibitors

dc.contributor.authorTaslimi, Parham
dc.contributor.authorAkıncıoğlu, Hülya
dc.contributor.authorGülçin, İlhami
dc.contributor.authorTaslimi, Parham
dc.date.accessioned2019-05-17T08:25:32Z
dc.date.available2019-05-17T08:25:32Z
dc.date.created2017
dc.date.issued2017
dc.date.issuedyyyymmdd2017-11
dc.departmentFakülteler, Fen Fakültesi, Biyoteknoloji Bölümü
dc.description.abstractIn this paper, synephrine and phenylephrine compounds showed excellent inhibitory effects against human carbonic anhydrase (hCA) isoforms I and II, -amylase, -glycosidase, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). Synephrine and phenylephrine had K-i values of 199.02 +/- 16.01 and 65.01 +/- 5.00M against hCA I and 336.02 +/- 74.01 and 92.04 +/- 18.03M against hCA II, respectively. On the other hand, their K-i values were found to be 169.10 +/- 80.03 and 88.03 +/- 5.01nM against AChE and 177.06 +/- 6.01 and 78.03 +/- 3.05nM against BChE, respectively. -Amylase and -glycosidase enzymes were easily inhibited by these compounds. -Glycosidase inhibitors, generally defined to as starch blockers, are anti-diabetic drugs that help to decrease post comestible blood glucose levels.
dc.identifier.doi10.1002/jbt.21973
dc.identifier.issue11
dc.identifier.startpagee21973
dc.identifier.urihttps://hdl.handle.net/11772/1199
dc.identifier.volume31
dc.language.isoen
dc.publisherWiley
dc.relation.ispartofJournal of Biochemical and Molecular Toxicology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectAlpha-amylase
dc.subjectAlpha-glycosidase
dc.subjectCarbonic anhydrase
dc.subjectPhenylephrine
dc.subjectSynephrine
dc.titleSynephrine and phenylephrine act as -amylase, -glycosidase, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase enzymes inhibitors
dc.typeArticle
dspace.entity.typePublication
relation.isAuthorOfPublicationdadfa319-65b8-4543-92b4-bea49e0139e9
relation.isAuthorOfPublication.latestForDiscoverydadfa319-65b8-4543-92b4-bea49e0139e9

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