Matches in SemOpenAlex for { <https://semopenalex.org/work/W1569018917> ?p ?o ?g. }
Showing items 1 to 90 of
90
with 100 items per page.
- W1569018917 endingPage "90" @default.
- W1569018917 startingPage "73" @default.
- W1569018917 abstract "This paper deals with studying biosynthetic pathways of 2 H-labeled purine ribonucleoside inosine excreted into liquid microbial culture (LC) by Gram-positive chemoheterotrophic bacterium Bacillus subtilis B-3157 while growing of this bacterium on heavy water (HW) medium with 2% (v/v) hydrolysate of deuterated biomass of the methylotrophic bacterium Brevibacterium methylicum B-5662 as a source of 2 H-labeled growth substrates. Isolation of 2 H-labeled inosine from LC was performed by adsorption/desorption on activated carbon with following extraction by 0.3 M ammonium–formate buffer (pH = 8.9), crystallization in 80% (v/v) EtOH, and ion exchange chromatography (IEC) on a column with AG50WX 4 cation exchange resin equilibrated with 0.3 M ammonium–formate buffer and 0.045 M NH 4 Cl. The investigation of deuterium incorporation into the inosine molecule by FAB method demonstrated incorporation of 5 deuterium atoms into the molecule (the total level of deuterium enrichment – 65.5 atom% 2 H) with 3 deuterium atoms being included into the ribose and 2 deuterium atoms – into the hypoxanthine residue of the molecule. Three non-exchangeable deuterium atoms were incorporated into the ribose residue owing to the preservation in this bacterium the minor pathways of de novo glucose biosynthesis in 2 H 2 O-medium. These non-exchangeable deuterium atoms in the ribose residue were originated from HMP shunt reactions, while two other deuterium atoms at C2,C8-positions in the hypoxanthine residue were synthesized from [ 2 H]amino acids, primarily glutamine and glycine, that originated from deuterated hydrolysate. A glycoside proton at b-N 9 -glycosidic bond could be replaced with deuterium via the reaction of ?? 2 elimination at the stage of ribulose-5-monophosphate formation from 3-keto-6-phosphogluconic acid with subsequent proton (deuteron) attachment at the ?1-position of ribulose-5-monophosphate. Two other protons at C2(C3) and C4 positions in ribose residue could be replaced with deuterium via further enzimatic isomerization of ribulose-5-monophosphate into ribose-5-monophosphate. Key words : 2 H-labeled inosine, biosynthesis, biosynthetic pathways, heavy water, Bacillus subtilis" @default.
- W1569018917 created "2016-06-24" @default.
- W1569018917 creator A5002118934 @default.
- W1569018917 creator A5067194907 @default.
- W1569018917 date "2014-01-01" @default.
- W1569018917 modified "2023-09-22" @default.
- W1569018917 title "Studying Biosynthetic Pathways of 2H-Labeled Purine Ribonucleoside Inosine in a Bacterium Bacillus Subtilis B-3157 by FAB Method" @default.
- W1569018917 hasPublicationYear "2014" @default.
- W1569018917 type Work @default.
- W1569018917 sameAs 1569018917 @default.
- W1569018917 citedByCount "19" @default.
- W1569018917 countsByYear W15690189172014 @default.
- W1569018917 countsByYear W15690189172016 @default.
- W1569018917 countsByYear W15690189172020 @default.
- W1569018917 countsByYear W15690189172021 @default.
- W1569018917 crossrefType "journal-article" @default.
- W1569018917 hasAuthorship W1569018917A5002118934 @default.
- W1569018917 hasAuthorship W1569018917A5067194907 @default.
- W1569018917 hasConcept C121332964 @default.
- W1569018917 hasConcept C162356407 @default.
- W1569018917 hasConcept C175605896 @default.
- W1569018917 hasConcept C181199279 @default.
- W1569018917 hasConcept C185592680 @default.
- W1569018917 hasConcept C2775986502 @default.
- W1569018917 hasConcept C2777272437 @default.
- W1569018917 hasConcept C2777610669 @default.
- W1569018917 hasConcept C2778386651 @default.
- W1569018917 hasConcept C2779461342 @default.
- W1569018917 hasConcept C2781116151 @default.
- W1569018917 hasConcept C28800991 @default.
- W1569018917 hasConcept C43617362 @default.
- W1569018917 hasConcept C523546767 @default.
- W1569018917 hasConcept C54355233 @default.
- W1569018917 hasConcept C55493867 @default.
- W1569018917 hasConcept C58364064 @default.
- W1569018917 hasConcept C62520636 @default.
- W1569018917 hasConcept C71240020 @default.
- W1569018917 hasConcept C86803240 @default.
- W1569018917 hasConcept C94412978 @default.
- W1569018917 hasConceptScore W1569018917C121332964 @default.
- W1569018917 hasConceptScore W1569018917C162356407 @default.
- W1569018917 hasConceptScore W1569018917C175605896 @default.
- W1569018917 hasConceptScore W1569018917C181199279 @default.
- W1569018917 hasConceptScore W1569018917C185592680 @default.
- W1569018917 hasConceptScore W1569018917C2775986502 @default.
- W1569018917 hasConceptScore W1569018917C2777272437 @default.
- W1569018917 hasConceptScore W1569018917C2777610669 @default.
- W1569018917 hasConceptScore W1569018917C2778386651 @default.
- W1569018917 hasConceptScore W1569018917C2779461342 @default.
- W1569018917 hasConceptScore W1569018917C2781116151 @default.
- W1569018917 hasConceptScore W1569018917C28800991 @default.
- W1569018917 hasConceptScore W1569018917C43617362 @default.
- W1569018917 hasConceptScore W1569018917C523546767 @default.
- W1569018917 hasConceptScore W1569018917C54355233 @default.
- W1569018917 hasConceptScore W1569018917C55493867 @default.
- W1569018917 hasConceptScore W1569018917C58364064 @default.
- W1569018917 hasConceptScore W1569018917C62520636 @default.
- W1569018917 hasConceptScore W1569018917C71240020 @default.
- W1569018917 hasConceptScore W1569018917C86803240 @default.
- W1569018917 hasConceptScore W1569018917C94412978 @default.
- W1569018917 hasLocation W15690189171 @default.
- W1569018917 hasOpenAccess W1569018917 @default.
- W1569018917 hasPrimaryLocation W15690189171 @default.
- W1569018917 hasRelatedWork W1484692103 @default.
- W1569018917 hasRelatedWork W1484883584 @default.
- W1569018917 hasRelatedWork W1486288254 @default.
- W1569018917 hasRelatedWork W1497944282 @default.
- W1569018917 hasRelatedWork W1506970664 @default.
- W1569018917 hasRelatedWork W1508195059 @default.
- W1569018917 hasRelatedWork W1510902715 @default.
- W1569018917 hasRelatedWork W1549231891 @default.
- W1569018917 hasRelatedWork W1552114712 @default.
- W1569018917 hasRelatedWork W1563290390 @default.
- W1569018917 hasRelatedWork W1642287326 @default.
- W1569018917 hasRelatedWork W1652772165 @default.
- W1569018917 hasRelatedWork W2017238434 @default.
- W1569018917 hasRelatedWork W2025533709 @default.
- W1569018917 hasRelatedWork W2094467764 @default.
- W1569018917 hasRelatedWork W2276231149 @default.
- W1569018917 hasRelatedWork W2288364529 @default.
- W1569018917 hasRelatedWork W2314672623 @default.
- W1569018917 hasRelatedWork W2314782063 @default.
- W1569018917 hasRelatedWork W2186544649 @default.
- W1569018917 hasVolume "1" @default.
- W1569018917 isParatext "false" @default.
- W1569018917 isRetracted "false" @default.
- W1569018917 magId "1569018917" @default.
- W1569018917 workType "article" @default.