Matches in SemOpenAlex for { <https://semopenalex.org/work/W4289950910> ?p ?o ?g. }
Showing items 1 to 58 of
58
with 100 items per page.
- W4289950910 endingPage "50" @default.
- W4289950910 startingPage "345" @default.
- W4289950910 abstract "Partially purified calf brain uridine kinase precipitated by bivalent metal cations has been compared with the soluble enzyme fraction regarding its stability in the presence of inactivating factors. The freeze-dried preparations of uridine kinase precipitaated by Pb2+ or Zn2+ ions, althouth enzymatically highly active, are insoluble in aqueous solutions. The activity of metal-insolubilized enzymes disappears during their preincubation in acidic media or in the presence of silver ions. Also trypsin, chymotrypsin and cathepsin B1 caused decreases in enzyme activity. However, fractions which have been precipitated by metal ions and freeze-dried are stable at high temperatures, whereas the activity of soluble uridine kinase is completely lost. Both unheated metal-ion precipitated uridine kinase preparations and those heated at 100 degrees C are equally sensitive to the feedback inhibition by CTP." @default.
- W4289950910 created "2022-08-06" @default.
- W4289950910 creator A5085670391 @default.
- W4289950910 date "1976-03-01" @default.
- W4289950910 modified "2023-09-29" @default.
- W4289950910 title "Stability of the insoluble form of uridine kinase coupled to zn2+ or pb2+ ions." @default.
- W4289950910 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8366" @default.
- W4289950910 hasPublicationYear "1976" @default.
- W4289950910 type Work @default.
- W4289950910 citedByCount "1" @default.
- W4289950910 crossrefType "journal-article" @default.
- W4289950910 hasAuthorship W4289950910A5085670391 @default.
- W4289950910 hasConcept C104317684 @default.
- W4289950910 hasConcept C178790620 @default.
- W4289950910 hasConcept C179104552 @default.
- W4289950910 hasConcept C181199279 @default.
- W4289950910 hasConcept C185592680 @default.
- W4289950910 hasConcept C199164860 @default.
- W4289950910 hasConcept C2778401398 @default.
- W4289950910 hasConcept C2780340462 @default.
- W4289950910 hasConcept C2781259782 @default.
- W4289950910 hasConcept C43617362 @default.
- W4289950910 hasConcept C544153396 @default.
- W4289950910 hasConcept C55493867 @default.
- W4289950910 hasConcept C67705224 @default.
- W4289950910 hasConceptScore W4289950910C104317684 @default.
- W4289950910 hasConceptScore W4289950910C178790620 @default.
- W4289950910 hasConceptScore W4289950910C179104552 @default.
- W4289950910 hasConceptScore W4289950910C181199279 @default.
- W4289950910 hasConceptScore W4289950910C185592680 @default.
- W4289950910 hasConceptScore W4289950910C199164860 @default.
- W4289950910 hasConceptScore W4289950910C2778401398 @default.
- W4289950910 hasConceptScore W4289950910C2780340462 @default.
- W4289950910 hasConceptScore W4289950910C2781259782 @default.
- W4289950910 hasConceptScore W4289950910C43617362 @default.
- W4289950910 hasConceptScore W4289950910C544153396 @default.
- W4289950910 hasConceptScore W4289950910C55493867 @default.
- W4289950910 hasConceptScore W4289950910C67705224 @default.
- W4289950910 hasIssue "3" @default.
- W4289950910 hasLocation W42899509101 @default.
- W4289950910 hasOpenAccess W4289950910 @default.
- W4289950910 hasPrimaryLocation W42899509101 @default.
- W4289950910 hasRelatedWork W1510792652 @default.
- W4289950910 hasRelatedWork W2020823886 @default.
- W4289950910 hasRelatedWork W2054443300 @default.
- W4289950910 hasRelatedWork W2063501700 @default.
- W4289950910 hasRelatedWork W2078595220 @default.
- W4289950910 hasRelatedWork W2097392642 @default.
- W4289950910 hasRelatedWork W2331831135 @default.
- W4289950910 hasRelatedWork W2436552255 @default.
- W4289950910 hasRelatedWork W2952322977 @default.
- W4289950910 hasRelatedWork W2952765157 @default.
- W4289950910 hasVolume "357" @default.
- W4289950910 isParatext "false" @default.
- W4289950910 isRetracted "false" @default.
- W4289950910 workType "article" @default.