Please use this identifier to cite or link to this item: https://hdl.handle.net/11000/30666
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dc.contributor.authorMonroy Noyola, Antonio-
dc.contributor.authorSOGORB, MIGUEL A-
dc.contributor.authorALMENARES LOPEZ, DAMIANYS-
dc.contributor.authorVilanova, Eugenio-
dc.contributor.otherDepartamentos de la UMH::Biología Aplicadaes_ES
dc.date.accessioned2024-01-26T09:23:50Z-
dc.date.available2024-01-26T09:23:50Z-
dc.date.created2021-05-
dc.identifier.citationInteracciones químico-biológicas Volume 345, 25 August (2021)es_ES
dc.identifier.issn0009-2797-
dc.identifier.urihttps://hdl.handle.net/11000/30666-
dc.description.abstractO-hexyl O-2,5-dichlorophenyl phosphoramidate (HDCP) induces delayed neuropathy. The R (+)-HDCP inhibits and caused the so call “aging reaction” on inhibited-NTE. This enantiomer is not hydrolyzed by Ca(II)-dependent A-esterases in mammal tissues but is hydrolyzed by Cu(II)-dependent chicken serum albumin (CSA). With the aim of identifying HDCP hydrolysis by other vertebrate albumins, we incubated albumin with 400 μM racemic HDCP in the presence of 100 μM copper sulfate. HDCPase activity was assessed by measurement of HDCP with chiral chromatography. Human, sheep, dog, pig, lamprey or cobra serum albumin did not show a significant activity (~10%). Rabbit and bovine albumins hydrolyzed both enantiomers of HDCP (25% and 50% respectively). Turkey serum albumin had more HDCPase activity (~80 μM remaining) than the chicken albumin (~150 μM remaining). No animal albumins other than chicken showed stereoselective hydrolysis. Preincubation of chicken albumin with 1 mM the histidine modifying agents, 100 μM N-bromosuccinimide (NBS) and Zn(II), inhibited its Cu(II)-dependent R (+)-HDCPase activity, where as other mM amino acids modifiers had no inhibitory effects. . These results confirm that the stereoselective hydrolysis of (+)-HDCP is a specific A-esterase catalytic property of chicken albumin. The higher HDCPase activity by turkey albumin suggests the amino-terminal sequence of avian albumins (DAEHK) is the active center of this Cu(II)-dependent A-esterase activity.es_ES
dc.formatapplication/pdfes_ES
dc.format.extent5es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.rightsinfo:eu-repo/semantics/closedAccesses_ES
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectAlbuminses_ES
dc.subjectPhosphoramidateses_ES
dc.subjectCopperes_ES
dc.subjectA-esteraseses_ES
dc.subjectStereoselectivityes_ES
dc.subjectHydrolysises_ES
dc.subject.otherCDU::5 - Ciencias puras y naturales::57 - Biología::573 - Biología general y teóricaes_ES
dc.titleDAEH N-terminal sequence of avian serum albumins as catalytic center of Cu (II)-dependent organophosphorus hydrolyzing A-esterase activityes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherversionhttps://doi.org/10.1016/j.cbi.2021.109524es_ES
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