Matches in SemOpenAlex for { <https://semopenalex.org/work/W2071566999> ?p ?o ?g. }
Showing items 1 to 53 of
53
with 100 items per page.
- W2071566999 endingPage "712" @default.
- W2071566999 startingPage "706" @default.
- W2071566999 abstract "Using the phthaloyl method, 18 γ-L-glutamyl peptides labelled with 14 C in the N-terminal position have been synthesized. The products were isolated by simple procedures using a Dowex-1 column or high voltage electrophoresis. The synthetic peptides contain minor impurities of the corresponding D-glutamyl isomers. The proportion of D-isomer was determined by the use of glutamic decarboxylase, or by a new method using digestion with purified γ-glutamyl cyclotransferase and determination of the resulting 2-pyrrolidone-5-carboxylic acid (5-oxoproline). Evidence was obtained that γ-glutamyl cyclotransferase acts only on the L-form of γ-glutamyl substrates; the enzyme could, therefore, be used for preparation of γ-D-glutamyl peptides from their racemic mixtures. The specificity of γ-glutamyl cyclotransferase has been examined using pure enzyme prepared from pig liver, and extracts from tissues of rat and man. The basic structural requirement in substrates may be represented as γ-L-glutamyl—NH—CHR—COOH. The amino acid linked to the γ-glutamyl group must be in the L configuration." @default.
- W2071566999 created "2016-06-24" @default.
- W2071566999 creator A5020254512 @default.
- W2071566999 creator A5026985685 @default.
- W2071566999 date "1975-06-01" @default.
- W2071566999 modified "2023-10-03" @default.
- W2071566999 title "Specificity of γ-Glutamyl Cyclotransferase" @default.
- W2071566999 doi "https://doi.org/10.1139/o75-097" @default.
- W2071566999 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/237623" @default.
- W2071566999 hasPublicationYear "1975" @default.
- W2071566999 type Work @default.
- W2071566999 sameAs 2071566999 @default.
- W2071566999 citedByCount "15" @default.
- W2071566999 countsByYear W20715669992021 @default.
- W2071566999 crossrefType "journal-article" @default.
- W2071566999 hasAuthorship W2071566999A5020254512 @default.
- W2071566999 hasAuthorship W2071566999A5026985685 @default.
- W2071566999 hasConcept C181199279 @default.
- W2071566999 hasConcept C185592680 @default.
- W2071566999 hasConcept C2779281246 @default.
- W2071566999 hasConcept C43617362 @default.
- W2071566999 hasConcept C515207424 @default.
- W2071566999 hasConcept C55493867 @default.
- W2071566999 hasConcept C71240020 @default.
- W2071566999 hasConceptScore W2071566999C181199279 @default.
- W2071566999 hasConceptScore W2071566999C185592680 @default.
- W2071566999 hasConceptScore W2071566999C2779281246 @default.
- W2071566999 hasConceptScore W2071566999C43617362 @default.
- W2071566999 hasConceptScore W2071566999C515207424 @default.
- W2071566999 hasConceptScore W2071566999C55493867 @default.
- W2071566999 hasConceptScore W2071566999C71240020 @default.
- W2071566999 hasIssue "6" @default.
- W2071566999 hasLocation W20715669991 @default.
- W2071566999 hasLocation W20715669992 @default.
- W2071566999 hasOpenAccess W2071566999 @default.
- W2071566999 hasPrimaryLocation W20715669991 @default.
- W2071566999 hasRelatedWork W1644178486 @default.
- W2071566999 hasRelatedWork W1983661517 @default.
- W2071566999 hasRelatedWork W1993694127 @default.
- W2071566999 hasRelatedWork W2004312381 @default.
- W2071566999 hasRelatedWork W2035595254 @default.
- W2071566999 hasRelatedWork W2065377794 @default.
- W2071566999 hasRelatedWork W2092435230 @default.
- W2071566999 hasRelatedWork W2130832373 @default.
- W2071566999 hasRelatedWork W2367275342 @default.
- W2071566999 hasRelatedWork W4242974861 @default.
- W2071566999 hasVolume "53" @default.
- W2071566999 isParatext "false" @default.
- W2071566999 isRetracted "false" @default.
- W2071566999 magId "2071566999" @default.
- W2071566999 workType "article" @default.