Rajesh, Ramanna V. ; Layer, Paul G. ; Boopathy, Rathanam (2009)
High aryl acylamidase activity associated with cobra venom acetylcholinesterase: biological significance.
In: Biochimie, 91 (11-12)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
Investigation of the non-classical functions of cholinesterases (ChEs) has been the subject of interest in the past three decades. One of which is aryl acylamidase (AAA) activity associated with ChEs, but characterized in in vitro, as an enzyme, splitting the artificial substrate o-nitroacetanilide with unknown physiological function. In the present study, we have compared levels of AAA activity of AChE from different sources like goat brain, electric eel organ and from venoms of different snakes. Remarkably cobra venom showed the highest AAA activity and also high AAA/AChE ratio. Both serotonergenic and cholinergic inhibitors inhibited the cobra venom AAA activity in a concentration dependent manner, which also underlines the association of AAA with AChE of cobra venom. The study becomes interesting because of i) the cobra venom AChE exists in monomeric globular forms; ii) in Alzheimer's disease too the most abundant forms of cholinesterases are monomeric globular forms, thought to be involved in the pathogenesis of Alzheimer's disease; iii) the effect of Alzheimer's disease drugs on the AAA activity of cobra venom, indicated that AAA activity of cobra venom was more sensitive than AChE and iv) Huperzine and Tacrine showed more pronounced effect on AAA. Thus, this study elucidates the high AAA associated with cobra venom AChE may serve as one of the prominent activity to test the pharmacological effect of AD drugs, as other sources were found to have lower activity.
Typ des Eintrags: | Artikel |
---|---|
Erschienen: | 2009 |
Autor(en): | Rajesh, Ramanna V. ; Layer, Paul G. ; Boopathy, Rathanam |
Art des Eintrags: | Bibliographie |
Titel: | High aryl acylamidase activity associated with cobra venom acetylcholinesterase: biological significance. |
Sprache: | Englisch |
Publikationsjahr: | 2009 |
Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Biochimie |
Jahrgang/Volume einer Zeitschrift: | 91 |
(Heft-)Nummer: | 11-12 |
Kurzbeschreibung (Abstract): | Investigation of the non-classical functions of cholinesterases (ChEs) has been the subject of interest in the past three decades. One of which is aryl acylamidase (AAA) activity associated with ChEs, but characterized in in vitro, as an enzyme, splitting the artificial substrate o-nitroacetanilide with unknown physiological function. In the present study, we have compared levels of AAA activity of AChE from different sources like goat brain, electric eel organ and from venoms of different snakes. Remarkably cobra venom showed the highest AAA activity and also high AAA/AChE ratio. Both serotonergenic and cholinergic inhibitors inhibited the cobra venom AAA activity in a concentration dependent manner, which also underlines the association of AAA with AChE of cobra venom. The study becomes interesting because of i) the cobra venom AChE exists in monomeric globular forms; ii) in Alzheimer's disease too the most abundant forms of cholinesterases are monomeric globular forms, thought to be involved in the pathogenesis of Alzheimer's disease; iii) the effect of Alzheimer's disease drugs on the AAA activity of cobra venom, indicated that AAA activity of cobra venom was more sensitive than AChE and iv) Huperzine and Tacrine showed more pronounced effect on AAA. Thus, this study elucidates the high AAA associated with cobra venom AChE may serve as one of the prominent activity to test the pharmacological effect of AD drugs, as other sources were found to have lower activity. |
Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie ?? fb10_zoologie ?? 10 Fachbereich Biologie > Developmental Biology and Neurogenetics |
Hinterlegungsdatum: | 21 Nov 2011 10:52 |
Letzte Änderung: | 05 Mär 2013 09:56 |
PPN: | |
Export: | |
Suche nach Titel in: | TUfind oder in Google |
Frage zum Eintrag |
Optionen (nur für Redakteure)
Redaktionelle Details anzeigen |