Linked Life Data

7702560

Source:http://linkedlifedata.com/resource/pubmed/id/7702560

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SubjectPredicateObjectContext
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pubmed-article:7702560pubmed:dateCreated1995-4-28lld:pubmed
pubmed-article:7702560pubmed:abstractTextTwo acetylcholinesterases (AChE) differing in substrate and inhibitor specificities have been characterized in the medical leech (Hirudo medicinalis). A 'spontaneously-soluble' portion of AChE activity (SS-AChE) was recovered from haemolymph and from tissues dilacerated in low-salt buffer. A second portion of AChE activity was obtained after extraction of tissues in low-salt buffer alone or containing 1% Triton X-100 [detergent-soluble (DS-) AChE). Both enzymes were purified to homogeneity by affinity chromatography on edrophonium- and concanavalin A-Sepharose columns. Denaturing SDS/PAGE under reducing conditions gave one band at 30 kDa for purified SS-AChE and 66 kDa for DS-AChE. Sephadex G-200 chromatography indicated a molecular mass of 66 kDa for native SS-AChE and of 130 kDa for DS-AChE. SS-AChE showed a single peak sedimenting at 5.0 S in sucrose gradients with or without Triton X-100, suggesting that it was a hydrophylic monomer (G1). DS-AChE sedimented as a single 6.1-6.5 S peak in the presence of Triton X-100 and aggregated in the absence of detergent. A treatment with phosphatidylinositol-specific phospholipase C suppressed aggregation and gave a 7 S peak. DS-AChE was thus an amphiphilic glycolipid-anchored dimer. Substrate specificities were studied using p-nitrophenyl esters (acetate, propionate and butyrate) and corresponding thiocholine esters as substrates. SS-AChE displayed only limited variations in Km values with charged and uncharged substrates, suggesting a reduced influence of electrostatic interactions in the enzyme substrate affinity. By contrast, DS-AChE displayed higher Km values with uncharged than with charged substrates. SS-AChE was more sensitive to eserine and di-isopropyl fluorophosphate (IC50 5 x 10(-8) and 10(-8) M respectively) than DS-AChE (5 x 10(-7) and 5 x 10(-5) M.lld:pubmed
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pubmed-article:7702560pubmed:authorpubmed-author:GiovanniniEElld:pubmed
pubmed-article:7702560pubmed:authorpubmed-author:RostJJlld:pubmed
pubmed-article:7702560pubmed:authorpubmed-author:ToutantJ PJPlld:pubmed
pubmed-article:7702560pubmed:authorpubmed-author:TannerS ESElld:pubmed
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pubmed-article:7702560pubmed:volume306 ( Pt 3)lld:pubmed
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pubmed-article:7702560pubmed:authorsCompleteYlld:pubmed
pubmed-article:7702560pubmed:pagination687-92lld:pubmed
pubmed-article:7702560pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:7702560pubmed:year1995lld:pubmed
pubmed-article:7702560pubmed:articleTitleSolubilization, molecular forms, purification and substrate specificity of two acetylcholinesterases in the medicinal leech (Hirudo medicinalis).lld:pubmed
pubmed-article:7702560pubmed:affiliationDepartment of Experimental Medicine, University of Perugia, Italy.lld:pubmed
pubmed-article:7702560pubmed:publicationTypeJournal Articlelld:pubmed
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