FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1788339998> ?p ?o ?g. }

• W1788339998 endingPage "498" @default.
• W1788339998 startingPage "489" @default.
• W1788339998 abstract "Vesicles consisting of (Ca(2+)+Mg(2+))-dependent ATPase (adenosine triphosphatase), and lipid were prepared from sarcoplasmic reticulum of rabbit skeletal muscle. As with non-ionic detergents [le Maire, Møller & Tanford (1976) Biochemistry15, 2336-2342] the (Ca(2+)+Mg(2+))-dependent ATPase after solubilization by deoxycholate showed a pronounced tendency to form oligomers in gel-chromatographic experiments, when eluted in the presence of deoxycholate and phosphatidylcholine. To evaluate the functional significance of oligomer formation the properties of enzymically active preparations of ATPase, solubilized by deoxycholate, were studied. Such preparations were obtained at a protein concentration of 2.5mg/ml in the presence of a high salt concentration (0.4m-KCl) and sucrose (0.3m) in the solubilization medium. Analytical ultracentrifugation of solubilized ATPase showed one protein boundary moving at the same rate as gel-chromatographically prepared monomeric ATPase (s(20,w)=6.0S). From simultaneous measurements of the diffusion coefficient an apparent molecular weight of 133000 was calculated, consistent with solubilization of ATPase in predominantly monomeric form. The enzymic activity of deoxycholate-solubilized ATPase when measured directly in the solubilization medium at optimal Ca(2+) and MgATP concentrations was about 35-50% of that of vesicular ATPase. The dependence of enzymic activity on MgATP concentration indicated that the solubilized ATPase retained high-affinity binding of MgATP, but the presence of high concentrations of the nucleotide did not stimulate activity further, in contrast with that of vesicular ATPase. The dependence of enzymic activity on the free Ca(2+) concentration was essentially the same for both solubilized and vesicular forms, indicating that interaction of ATPase with more than one molecule of Ca(2+) is required for enzyme activity. Solubilized enzyme at 20 degrees C was phosphorylated to about the same degree as vesicular ATPase. It is concluded that the catalytic activity of monomeric ATPase retains most of the features of vesicular ATPase and that extensive oligomer formation in gel-chromatographic experiments in the presence of deoxycholate probably reflects processes taking place during inactivation and delipidation of the protein." @default.
• W1788339998 created "2016-06-24" @default.
• W1788339998 creator A5015360299 @default.
• W1788339998 creator A5068923513 @default.
• W1788339998 creator A5077132895 @default.
• W1788339998 creator A5090523158 @default.
• W1788339998 date "1978-03-01" @default.
• W1788339998 modified "2023-10-15" @default.
• W1788339998 title "The functional unit of calcium-plus-magnesium-ion-dependent adenosine triphosphatase from sarcoplasmic reticulum. The aggregational state of the deoxycholate-solubilized protein in an enzymically active form" @default.
• W1788339998 cites W1504121383 @default.
• W1788339998 cites W1505508735 @default.
• W1788339998 cites W1510897113 @default.
• W1788339998 cites W1513897103 @default.
• W1788339998 cites W1572315545 @default.
• W1788339998 cites W1581351937 @default.
• W1788339998 cites W1584803815 @default.
• W1788339998 cites W1592464016 @default.
• W1788339998 cites W1595204022 @default.
• W1788339998 cites W1602992567 @default.
• W1788339998 cites W1604248953 @default.
• W1788339998 cites W1618664245 @default.
• W1788339998 cites W1775749144 @default.
• W1788339998 cites W1985966625 @default.
• W1788339998 cites W2002885745 @default.
• W1788339998 cites W2006716381 @default.
• W1788339998 cites W2028503912 @default.
• W1788339998 cites W2037591099 @default.
• W1788339998 cites W2039485889 @default.
• W1788339998 cites W2061734875 @default.
• W1788339998 cites W2063821350 @default.
• W1788339998 cites W2074406795 @default.
• W1788339998 cites W2081014774 @default.
• W1788339998 cites W2104957768 @default.
• W1788339998 cites W2114439837 @default.
• W1788339998 cites W2146752257 @default.
• W1788339998 cites W2209681382 @default.
• W1788339998 cites W2414667409 @default.
• W1788339998 doi "https://doi.org/10.1042/bj1690489" @default.
• W1788339998 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1183821" @default.
• W1788339998 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/148271" @default.
• W1788339998 hasPublicationYear "1978" @default.
• W1788339998 type Work @default.
• W1788339998 sameAs 1788339998 @default.
• W1788339998 citedByCount "53" @default.
• W1788339998 countsByYear W17883399982014 @default.
• W1788339998 countsByYear W17883399982020 @default.
• W1788339998 crossrefType "journal-article" @default.
• W1788339998 hasAuthorship W1788339998A5015360299 @default.
• W1788339998 hasAuthorship W1788339998A5068923513 @default.
• W1788339998 hasAuthorship W1788339998A5077132895 @default.
• W1788339998 hasAuthorship W1788339998A5090523158 @default.
• W1788339998 hasBestOaLocation W17883399982 @default.
• W1788339998 hasConcept C101571972 @default.
• W1788339998 hasConcept C130316041 @default.
• W1788339998 hasConcept C158617107 @default.
• W1788339998 hasConcept C178790620 @default.
• W1788339998 hasConcept C181199279 @default.
• W1788339998 hasConcept C185592680 @default.
• W1788339998 hasConcept C23265538 @default.
• W1788339998 hasConcept C2777132085 @default.
• W1788339998 hasConcept C2778038992 @default.
• W1788339998 hasConcept C2778336440 @default.
• W1788339998 hasConcept C2779340330 @default.
• W1788339998 hasConcept C3018891471 @default.
• W1788339998 hasConcept C41625074 @default.
• W1788339998 hasConcept C43617362 @default.
• W1788339998 hasConcept C4863142 @default.
• W1788339998 hasConcept C519063684 @default.
• W1788339998 hasConcept C54689828 @default.
• W1788339998 hasConcept C55493867 @default.
• W1788339998 hasConcept C87644729 @default.
• W1788339998 hasConceptScore W1788339998C101571972 @default.
• W1788339998 hasConceptScore W1788339998C130316041 @default.
• W1788339998 hasConceptScore W1788339998C158617107 @default.
• W1788339998 hasConceptScore W1788339998C178790620 @default.
• W1788339998 hasConceptScore W1788339998C181199279 @default.
• W1788339998 hasConceptScore W1788339998C185592680 @default.
• W1788339998 hasConceptScore W1788339998C23265538 @default.
• W1788339998 hasConceptScore W1788339998C2777132085 @default.
• W1788339998 hasConceptScore W1788339998C2778038992 @default.
• W1788339998 hasConceptScore W1788339998C2778336440 @default.
• W1788339998 hasConceptScore W1788339998C2779340330 @default.
• W1788339998 hasConceptScore W1788339998C3018891471 @default.
• W1788339998 hasConceptScore W1788339998C41625074 @default.
• W1788339998 hasConceptScore W1788339998C43617362 @default.
• W1788339998 hasConceptScore W1788339998C4863142 @default.
• W1788339998 hasConceptScore W1788339998C519063684 @default.
• W1788339998 hasConceptScore W1788339998C54689828 @default.
• W1788339998 hasConceptScore W1788339998C55493867 @default.
• W1788339998 hasConceptScore W1788339998C87644729 @default.
• W1788339998 hasIssue "3" @default.
• W1788339998 hasLocation W17883399981 @default.
• W1788339998 hasLocation W17883399982 @default.
• W1788339998 hasLocation W17883399983 @default.
• W1788339998 hasLocation W17883399984 @default.
• W1788339998 hasOpenAccess W1788339998 @default.
• W1788339998 hasPrimaryLocation W17883399981 @default.
• W1788339998 hasRelatedWork W1970312064 @default.

• next