Matches in SemOpenAlex for { <https://semopenalex.org/work/W2022133134> ?p ?o ?g. }
Showing items 1 to 86 of
86
with 100 items per page.
- W2022133134 endingPage "502" @default.
- W2022133134 startingPage "497" @default.
- W2022133134 abstract "The asymmetric forms of acetylcholinesterase were purified from the electric organs of the electric rays Narke japonica and Torpedo californica, and their properties were compared. Asymmetric acetylcholinesterase was purified by immunoaffinity chromatography with a monoclonal antibody (Nj-601) to acetylcholinesterase. The MgCl2 extracts of these electric organs were applied to a column of Nj-601-Sepharose, and the bound acetylcholinesterase was eluted by lowering the pH of the eluent to 2.8. The purified asymmetric acetylcholinesterases gave peaks of 17 S (A12) and 13 S (A8) on sucrose density gradients. The enzyme from N. japonica contained more A8 than A12, while that of T. californica contained more A12. After treatment with collagenase, the enzymes gave three peaks on sedimentation; 20 S, 16 S and 11 S for N. japonica, and 19 S, 15 S and 11 S for T. californica, indicating the presence of collagen-like tails. On polyacrylamide gel electrophoresis in sodium dodecyl sulfate, the asymmetric acetylcholinesterase from N. japonica gave bands of Mr 140 000, 100 000, 70 000 and 60 000, while that from T. californica gave bands of Mr 140 000, 100 000, 70 000 and 55 000. The bands of Mr 70 000 and 140 000 were monomers and non-reducible dimers, respectively, of the catalytic subunits. The bands of Mr 60 000 and 55 000 were the tail subunits, since collagenase treatment of the purified enzymes markedly decreased the amounts of these components. The Mr 100 000 subunit constituted less than 3% of the total asymmetric acetylcholinesterase from N. japonica but 18% of that from T. californica. The tail subunits constituted 6-8% of the two preparations. The catalytic subunits and the Mr 100 000 subunits bound concanavalin A, indicating that they are glycoproteins. The amino acid compositions of the enzymes from N. japonica and T. californica were very similar. Both contained hydroxyproline and hydroxylysine, characteristic of the collagen-like tails. The enzyme required divalent metal ions for activity, but only Mn2+, Mg2+ and Ca2+ were effective. Mn2+ was effective at the lowest concentrations, while Mg2+ gave the highest activity." @default.
- W2022133134 created "2016-06-24" @default.
- W2022133134 creator A5003774739 @default.
- W2022133134 creator A5008344839 @default.
- W2022133134 creator A5081284691 @default.
- W2022133134 date "1985-12-01" @default.
- W2022133134 modified "2023-09-27" @default.
- W2022133134 title "Comparison of asymmetric forms of acetylcholinesterase from the electric organ of Narke japonica and Torpedo californica" @default.
- W2022133134 cites W1550706388 @default.
- W2022133134 cites W1584942338 @default.
- W2022133134 cites W1936620479 @default.
- W2022133134 cites W1983184188 @default.
- W2022133134 cites W2018272020 @default.
- W2022133134 cites W2021774717 @default.
- W2022133134 cites W2032182163 @default.
- W2022133134 cites W2035706400 @default.
- W2022133134 cites W2038415253 @default.
- W2022133134 cites W2050474795 @default.
- W2022133134 cites W2054749431 @default.
- W2022133134 cites W2100837269 @default.
- W2022133134 cites W2104606868 @default.
- W2022133134 cites W279983762 @default.
- W2022133134 cites W40534437 @default.
- W2022133134 doi "https://doi.org/10.1111/j.1432-1033.1985.tb09329.x" @default.
- W2022133134 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3000781" @default.
- W2022133134 hasPublicationYear "1985" @default.
- W2022133134 type Work @default.
- W2022133134 sameAs 2022133134 @default.
- W2022133134 citedByCount "8" @default.
- W2022133134 countsByYear W20221331342012 @default.
- W2022133134 crossrefType "journal-article" @default.
- W2022133134 hasAuthorship W2022133134A5003774739 @default.
- W2022133134 hasAuthorship W2022133134A5008344839 @default.
- W2022133134 hasAuthorship W2022133134A5081284691 @default.
- W2022133134 hasConcept C101660505 @default.
- W2022133134 hasConcept C116084860 @default.
- W2022133134 hasConcept C123419017 @default.
- W2022133134 hasConcept C153911025 @default.
- W2022133134 hasConcept C170493617 @default.
- W2022133134 hasConcept C181199279 @default.
- W2022133134 hasConcept C185592680 @default.
- W2022133134 hasConcept C2778394429 @default.
- W2022133134 hasConcept C2778816929 @default.
- W2022133134 hasConcept C2779409272 @default.
- W2022133134 hasConcept C43617362 @default.
- W2022133134 hasConcept C55493867 @default.
- W2022133134 hasConcept C59822182 @default.
- W2022133134 hasConcept C80161118 @default.
- W2022133134 hasConcept C86803240 @default.
- W2022133134 hasConceptScore W2022133134C101660505 @default.
- W2022133134 hasConceptScore W2022133134C116084860 @default.
- W2022133134 hasConceptScore W2022133134C123419017 @default.
- W2022133134 hasConceptScore W2022133134C153911025 @default.
- W2022133134 hasConceptScore W2022133134C170493617 @default.
- W2022133134 hasConceptScore W2022133134C181199279 @default.
- W2022133134 hasConceptScore W2022133134C185592680 @default.
- W2022133134 hasConceptScore W2022133134C2778394429 @default.
- W2022133134 hasConceptScore W2022133134C2778816929 @default.
- W2022133134 hasConceptScore W2022133134C2779409272 @default.
- W2022133134 hasConceptScore W2022133134C43617362 @default.
- W2022133134 hasConceptScore W2022133134C55493867 @default.
- W2022133134 hasConceptScore W2022133134C59822182 @default.
- W2022133134 hasConceptScore W2022133134C80161118 @default.
- W2022133134 hasConceptScore W2022133134C86803240 @default.
- W2022133134 hasIssue "3" @default.
- W2022133134 hasLocation W20221331341 @default.
- W2022133134 hasLocation W20221331342 @default.
- W2022133134 hasOpenAccess W2022133134 @default.
- W2022133134 hasPrimaryLocation W20221331341 @default.
- W2022133134 hasRelatedWork W113657298 @default.
- W2022133134 hasRelatedWork W1440031586 @default.
- W2022133134 hasRelatedWork W1649084527 @default.
- W2022133134 hasRelatedWork W1936620479 @default.
- W2022133134 hasRelatedWork W2074738418 @default.
- W2022133134 hasRelatedWork W2082067665 @default.
- W2022133134 hasRelatedWork W2109078573 @default.
- W2022133134 hasRelatedWork W2163536072 @default.
- W2022133134 hasRelatedWork W2324335556 @default.
- W2022133134 hasRelatedWork W2463802760 @default.
- W2022133134 hasVolume "153" @default.
- W2022133134 isParatext "false" @default.
- W2022133134 isRetracted "false" @default.
- W2022133134 magId "2022133134" @default.
- W2022133134 workType "article" @default.