FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2045825024> ?p ?o ?g. }

• W2045825024 endingPage "58" @default.
• W2045825024 startingPage "45" @default.
• W2045825024 abstract "A study of purine uptake, phosphoribosyltransferase activity and incorporation in a wild-type strain of yeast and a mutant resistant to 4-aminopyrazolo (3, 4-d) pyrimidine (4-APP) yielded the following results: 1. The mutant is resistant to 4-APP, 8-azaadenine, 6-mercaptopurine, 8-azaguanine and guanine, all of which inhibit growth of the wild-type strain. It also has a reduced growth rate and is not stimulated by exogenous adenine and hypoxanthine. 2. Purine phosphoribosyltransferase activities for adenine, hypoxanthine, guanine and 4-APP were 48–60% higher in the mutant than in the wild type. 3. Uptake of adenine and hypoxanthine by the mutant was lower than in wild type and the size of the purine pools was reduced. Guanine uptake and pool size were the same in the two strains. 4. The wild type was able to take up 4-APP from the medium; and to incorporate it into cold trichloroacetic acid-insoluble material. There was no detectable uptake of 4-APP by the mutant. 5. Uptake of adenine and hypoxanthine obeyed simple enzyme kinetics in both strains. The observed constants were (a) wild type: Km (adenine) 0.12·10−6 M; Vmax (adenine) 1.1·10−10 μmole·cell−1·min−1; (b) mutant: Km (adenine) 2.6·10−6 M Vmax (adenine) 0.61·10−10 μmole·cell−1·min−1; Km (hypoxanthine) 2.9·10−5 M; Vmax (hypoxanthine) 0.32·10−10 μmole·cell−1·min−1. 6. Uptake of adenine and hypoxanthine by wild type was competitively inhibited by purines and purine analogues. This inhibition was not found in experiments with the mutant. Uptake of guanine in both strains was inhibited by hypoxanthine but not by adenine. 7. Although uptake of adenine and hypoxanthine was reduced in the presence of 4-APP there was significant stimulation of their incorporation into cold trichloroacetic acid-insoluble material. These experiments indicate that there are at least two purine permeases in yeast: an “adenine permease” which also accepts hypoxanthine, 4-APP and some other analogues; and a “guanine permease” which accepts hypoxanthine and 8-azaguanine. It is proposed that in the mutant strain the specificity of the “adenine permease” is changed such that it now only accepts adenine as a substrate, whilst the specificity of the guanine permease is unaffected. The consequent exclusion of 4-APP and other analogues from the cells of the mutant strain would account for its resistance. Concomitant resistance to guanine and 8-azaguanine may indicate a change in the properties of the pathway for de novo purine synthesis. It is suggested that activity of the purine phosphoribosyltransferases may be related to the rate of purine uptake and the size of the purine pool." @default.
• W2045825024 created "2016-06-24" @default.
• W2045825024 creator A5028848699 @default.
• W2045825024 creator A5059437085 @default.
• W2045825024 date "1972-03-30" @default.
• W2045825024 modified "2023-09-25" @default.
• W2045825024 title "The uptake and incorporation of purines by wild-type Saccharomyces cerevisiae and a mutant resistant to 4-aminopyrazolo (3, 4-d) pyrimidine" @default.
• W2045825024 cites W1486602114 @default.
• W2045825024 cites W1557134918 @default.
• W2045825024 cites W1775749144 @default.
• W2045825024 cites W1914862821 @default.
• W2045825024 cites W1982458691 @default.
• W2045825024 cites W2003714719 @default.
• W2045825024 cites W2022419195 @default.
• W2045825024 cites W2026099271 @default.
• W2045825024 cites W2034188127 @default.
• W2045825024 cites W2051906930 @default.
• W2045825024 cites W2058405920 @default.
• W2045825024 cites W2148155113 @default.
• W2045825024 doi "https://doi.org/10.1016/0304-4165(72)90115-8" @default.
• W2045825024 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/4336666" @default.
• W2045825024 hasPublicationYear "1972" @default.
• W2045825024 type Work @default.
• W2045825024 sameAs 2045825024 @default.
• W2045825024 citedByCount "33" @default.
• W2045825024 crossrefType "journal-article" @default.
• W2045825024 hasAuthorship W2045825024A5028848699 @default.
• W2045825024 hasAuthorship W2045825024A5059437085 @default.
• W2045825024 hasConcept C104317684 @default.
• W2045825024 hasConcept C143065580 @default.
• W2045825024 hasConcept C153911025 @default.
• W2045825024 hasConcept C169586020 @default.
• W2045825024 hasConcept C181199279 @default.
• W2045825024 hasConcept C185592680 @default.
• W2045825024 hasConcept C207583985 @default.
• W2045825024 hasConcept C2776476023 @default.
• W2045825024 hasConcept C2777991568 @default.
• W2045825024 hasConcept C2778301229 @default.
• W2045825024 hasConcept C2779321679 @default.
• W2045825024 hasConcept C2781116151 @default.
• W2045825024 hasConcept C2909697302 @default.
• W2045825024 hasConcept C40507961 @default.
• W2045825024 hasConcept C512185932 @default.
• W2045825024 hasConcept C55493867 @default.
• W2045825024 hasConcept C78179603 @default.
• W2045825024 hasConcept C86803240 @default.
• W2045825024 hasConceptScore W2045825024C104317684 @default.
• W2045825024 hasConceptScore W2045825024C143065580 @default.
• W2045825024 hasConceptScore W2045825024C153911025 @default.
• W2045825024 hasConceptScore W2045825024C169586020 @default.
• W2045825024 hasConceptScore W2045825024C181199279 @default.
• W2045825024 hasConceptScore W2045825024C185592680 @default.
• W2045825024 hasConceptScore W2045825024C207583985 @default.
• W2045825024 hasConceptScore W2045825024C2776476023 @default.
• W2045825024 hasConceptScore W2045825024C2777991568 @default.
• W2045825024 hasConceptScore W2045825024C2778301229 @default.
• W2045825024 hasConceptScore W2045825024C2779321679 @default.
• W2045825024 hasConceptScore W2045825024C2781116151 @default.
• W2045825024 hasConceptScore W2045825024C2909697302 @default.
• W2045825024 hasConceptScore W2045825024C40507961 @default.
• W2045825024 hasConceptScore W2045825024C512185932 @default.
• W2045825024 hasConceptScore W2045825024C55493867 @default.
• W2045825024 hasConceptScore W2045825024C78179603 @default.
• W2045825024 hasConceptScore W2045825024C86803240 @default.
• W2045825024 hasIssue "1" @default.
• W2045825024 hasLocation W20458250241 @default.
• W2045825024 hasLocation W20458250242 @default.
• W2045825024 hasOpenAccess W2045825024 @default.
• W2045825024 hasPrimaryLocation W20458250241 @default.
• W2045825024 hasRelatedWork W1539181208 @default.
• W2045825024 hasRelatedWork W1949571784 @default.
• W2045825024 hasRelatedWork W1998498306 @default.
• W2045825024 hasRelatedWork W2013157260 @default.
• W2045825024 hasRelatedWork W2020908685 @default.
• W2045825024 hasRelatedWork W2045825024 @default.
• W2045825024 hasRelatedWork W2047689188 @default.
• W2045825024 hasRelatedWork W2064159418 @default.
• W2045825024 hasRelatedWork W2065885659 @default.
• W2045825024 hasRelatedWork W2127998943 @default.
• W2045825024 hasVolume "264" @default.
• W2045825024 isParatext "false" @default.
• W2045825024 isRetracted "false" @default.
• W2045825024 magId "2045825024" @default.
• W2045825024 workType "article" @default.