Matches in SemOpenAlex for { <https://semopenalex.org/work/W1921151864> ?p ?o ?g. }
Showing items 1 to 80 of
80
with 100 items per page.
- W1921151864 endingPage "571" @default.
- W1921151864 startingPage "565" @default.
- W1921151864 abstract "Iodoacetate is known to inhibit horse liver alcohol dehydrogenase by selectively reacting with Cys-46 in each of the two active sites of the dimeric enzyme. In this study, a method is described in which horse liver alcohol dehydrogenase is carboxymethylated while the enzyme is strongly bioaffinity-bound to N6-[N-(6-aminohexyl)carbamolymethyl]-NADH-substituted Sepharose 2B as a ternary complex in the presence of isobutyramide. A low degree of coenzyme-ligand substitution (about 20 nmol/ml settled gel) was used in order to restrict enzyme-coenzyme interaction on the gel to a single subunit. After the modification reaction by iodoacetate on the solid phase, the enzyme was eluted from the NADH-substituted gel and its properties studied in free solution. Based on the incorporation of [14C]carboxymethyl groups, it is concluded that the reaction takes place at the active center of the ‘free’ (not bioaffinity-bound) subunit; amino acid analysis showed that S-carboxymethylcysteine had been formed. Also, the monoalkylated enzyme preparation was half as active as native enzyme when ethanol or benzaldehyde were used as substrates. Furthermore, after alkylation on the solid phase the enzyme loses about 50% of its original NADH-binding capacity which was determined fluorometrically by titrating with NADH in the presence of isobutyramide. From these results it is suggested that both subunits in native horse liver alcohol dehydrogenase are kinetically equivalent." @default.
- W1921151864 created "2016-06-24" @default.
- W1921151864 creator A5002796202 @default.
- W1921151864 creator A5007955463 @default.
- W1921151864 date "1979-03-01" @default.
- W1921151864 modified "2023-09-28" @default.
- W1921151864 title "The Use of Biochemical Solid-Phase Techniques in the Study of Alcohol Dehydrogenase. 2. Selective Carboxymethylation of Bioaffinity-Bound Alcohol Dehydrogenase" @default.
- W1921151864 cites W1459088981 @default.
- W1921151864 cites W1508835854 @default.
- W1921151864 cites W1517436794 @default.
- W1921151864 cites W1578304546 @default.
- W1921151864 cites W1578627487 @default.
- W1921151864 cites W173753228 @default.
- W1921151864 cites W1775749144 @default.
- W1921151864 cites W1974053931 @default.
- W1921151864 cites W1979553533 @default.
- W1921151864 cites W1996131560 @default.
- W1921151864 cites W2010482530 @default.
- W1921151864 cites W2017470279 @default.
- W1921151864 cites W2017773577 @default.
- W1921151864 cites W2019884903 @default.
- W1921151864 cites W2026854579 @default.
- W1921151864 cites W2035626564 @default.
- W1921151864 cites W2053613947 @default.
- W1921151864 cites W2059717838 @default.
- W1921151864 cites W2073312123 @default.
- W1921151864 cites W2077742005 @default.
- W1921151864 cites W2093632569 @default.
- W1921151864 cites W2149085786 @default.
- W1921151864 cites W3085207721 @default.
- W1921151864 cites W940916854 @default.
- W1921151864 cites W3009733911 @default.
- W1921151864 doi "https://doi.org/10.1111/j.1432-1033.1979.tb12926.x" @default.
- W1921151864 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/218820" @default.
- W1921151864 hasPublicationYear "1979" @default.
- W1921151864 type Work @default.
- W1921151864 sameAs 1921151864 @default.
- W1921151864 citedByCount "15" @default.
- W1921151864 crossrefType "journal-article" @default.
- W1921151864 hasAuthorship W1921151864A5002796202 @default.
- W1921151864 hasAuthorship W1921151864A5007955463 @default.
- W1921151864 hasBestOaLocation W19211518641 @default.
- W1921151864 hasConcept C181199279 @default.
- W1921151864 hasConcept C185592680 @default.
- W1921151864 hasConcept C197957613 @default.
- W1921151864 hasConcept C2776317432 @default.
- W1921151864 hasConcept C2777344606 @default.
- W1921151864 hasConcept C2781066024 @default.
- W1921151864 hasConcept C55493867 @default.
- W1921151864 hasConcept C71240020 @default.
- W1921151864 hasConceptScore W1921151864C181199279 @default.
- W1921151864 hasConceptScore W1921151864C185592680 @default.
- W1921151864 hasConceptScore W1921151864C197957613 @default.
- W1921151864 hasConceptScore W1921151864C2776317432 @default.
- W1921151864 hasConceptScore W1921151864C2777344606 @default.
- W1921151864 hasConceptScore W1921151864C2781066024 @default.
- W1921151864 hasConceptScore W1921151864C55493867 @default.
- W1921151864 hasConceptScore W1921151864C71240020 @default.
- W1921151864 hasIssue "2" @default.
- W1921151864 hasLocation W19211518641 @default.
- W1921151864 hasLocation W19211518642 @default.
- W1921151864 hasOpenAccess W1921151864 @default.
- W1921151864 hasPrimaryLocation W19211518641 @default.
- W1921151864 hasRelatedWork W2010400501 @default.
- W1921151864 hasRelatedWork W2057531719 @default.
- W1921151864 hasRelatedWork W2081069687 @default.
- W1921151864 hasRelatedWork W2083360052 @default.
- W1921151864 hasRelatedWork W2111297576 @default.
- W1921151864 hasRelatedWork W2143734654 @default.
- W1921151864 hasRelatedWork W2161994171 @default.
- W1921151864 hasRelatedWork W2170874906 @default.
- W1921151864 hasRelatedWork W2886629824 @default.
- W1921151864 hasRelatedWork W628555867 @default.
- W1921151864 hasVolume "94" @default.
- W1921151864 isParatext "false" @default.
- W1921151864 isRetracted "false" @default.
- W1921151864 magId "1921151864" @default.
- W1921151864 workType "article" @default.