FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4289968104> ?p ?o ?g. }

• W4289968104 endingPage "31" @default.
• W4289968104 startingPage "1216" @default.
• W4289968104 abstract "Biosynthetic L-threonine dehydratase was purified to homogeneous state with yield 29% of total activity from E. coli K-12. The cells were disrupted by means of ultra sound. Nucleic acids and nucleoproteins were precipitated with protamine sulphate, the proteins were fractioned with (NH4)2SO4, by gel filtration through Sephadex G-25 followed by chromatography on DEAE-cellulose using stepways elution by changing the pH-values. The homogenity of the enzyme was shown by polyacrylamide gel disc electrophoresis in the presence of dodecylsulphate. The enzyme consists of equal subunits having a molecular weight about 57000. The polyacrylamide gel disc electrophoresis had shown that the native enzyme consists of a set of oligomeric forms. The multiplisity of molecular organization of the enzyme was relfected in complicated kinetic behavior: at pH greater than 9 on the plots of initial reaction rate (upsilon) versus initial substrate concentration ([S]0) there were four inflexion points (two intermediate plateaux) the position and deepness of which depended on enzyme concentration. Kinetic properties of the highly purified enzyme and the enzyme in crude cell extracts at pH 9.3 and 7.4 were identical. At pH 8,3 on the upsilon versus [S]0 plots appeared two inflexion points (one intermediate plateau), the position of which practically did not depend on enzyme concentration in the reaction mixture but strongly depended on the enzyme concentration in the stock solution. Repeated polyacrylamide gel disc electrophoresis of several oligomeric forms isolated by the first electrophoresis had shown that oligomeric forms underwent a slow polymerization. It is suggested that biosynthetic L-threonine dehydratase from E. coli K-12 is a set of multiple oligomeric forms having different kinetic parameters. Probably, each form of the enzyme has a simple kinetics characterized by hyperbolic or sigmoidal shape of upsilon versus [S]0 plots. The rate of equilibrium between the oligomeric forms is small in comparison with the enzyme reaction velosity, that lead to the complex kinetic curves appearing as a result of summing up the kinetics inherent to the individual forms." @default.
• W4289968104 created "2022-08-06" @default.
• W4289968104 creator A5044952107 @default.
• W4289968104 creator A5053517539 @default.
• W4289968104 creator A5071816029 @default.
• W4289968104 creator A5079902438 @default.
• W4289968104 creator A5085755760 @default.
• W4289968104 date "1975-11-01" @default.
• W4289968104 modified "2023-09-29" @default.
• W4289968104 title "[Purification, molecular multiplicity and kinetic properties of biosynthetic L-threonine dehydratase from E. coli K-12]." @default.
• W4289968104 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2333" @default.
• W4289968104 hasPublicationYear "1975" @default.
• W4289968104 type Work @default.
• W4289968104 citedByCount "0" @default.
• W4289968104 crossrefType "journal-article" @default.
• W4289968104 hasAuthorship W4289968104A5044952107 @default.
• W4289968104 hasAuthorship W4289968104A5053517539 @default.
• W4289968104 hasAuthorship W4289968104A5071816029 @default.
• W4289968104 hasAuthorship W4289968104A5079902438 @default.
• W4289968104 hasAuthorship W4289968104A5085755760 @default.
• W4289968104 hasConcept C101660505 @default.
• W4289968104 hasConcept C116084860 @default.
• W4289968104 hasConcept C163994747 @default.
• W4289968104 hasConcept C181199279 @default.
• W4289968104 hasConcept C185592680 @default.
• W4289968104 hasConcept C188027245 @default.
• W4289968104 hasConcept C193363816 @default.
• W4289968104 hasConcept C2778862431 @default.
• W4289968104 hasConcept C28212737 @default.
• W4289968104 hasConcept C43617362 @default.
• W4289968104 hasConcept C55493867 @default.
• W4289968104 hasConceptScore W4289968104C101660505 @default.
• W4289968104 hasConceptScore W4289968104C116084860 @default.
• W4289968104 hasConceptScore W4289968104C163994747 @default.
• W4289968104 hasConceptScore W4289968104C181199279 @default.
• W4289968104 hasConceptScore W4289968104C185592680 @default.
• W4289968104 hasConceptScore W4289968104C188027245 @default.
• W4289968104 hasConceptScore W4289968104C193363816 @default.
• W4289968104 hasConceptScore W4289968104C2778862431 @default.
• W4289968104 hasConceptScore W4289968104C28212737 @default.
• W4289968104 hasConceptScore W4289968104C43617362 @default.
• W4289968104 hasConceptScore W4289968104C55493867 @default.
• W4289968104 hasIssue "6" @default.
• W4289968104 hasLocation W42899681041 @default.
• W4289968104 hasOpenAccess W4289968104 @default.
• W4289968104 hasPrimaryLocation W42899681041 @default.
• W4289968104 hasRelatedWork W127938976 @default.
• W4289968104 hasRelatedWork W1521506765 @default.
• W4289968104 hasRelatedWork W1557733310 @default.
• W4289968104 hasRelatedWork W1649084527 @default.
• W4289968104 hasRelatedWork W1823025905 @default.
• W4289968104 hasRelatedWork W1923316703 @default.
• W4289968104 hasRelatedWork W1943335296 @default.
• W4289968104 hasRelatedWork W2003005087 @default.
• W4289968104 hasRelatedWork W2338928806 @default.
• W4289968104 hasRelatedWork W2336442873 @default.
• W4289968104 hasVolume "40" @default.
• W4289968104 isParatext "false" @default.
• W4289968104 isRetracted "false" @default.
• W4289968104 workType "article" @default.