FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2079776446> ?p ?o ?g. }

• W2079776446 endingPage "5066" @default.
• W2079776446 startingPage "5057" @default.
• W2079776446 abstract "The kinetics of thermally induced aggregation of the glycoprotein Peniophora lycii phytase (Phy) and a deglycosylated form (dgPhy) was studied by dynamic (DLS) and static (SLS) light scattering. This provided a detailed insight into the time course of the formation of small aggregates (∼10−100 molecules) of the enzyme. The thermodynamic stability of the two forms was also investigated using scanning calorimetry (DSC). It was found that the glycans strongly promoted kinetic stability (i.e., reduced the rate of irreversible denaturation) while leaving the equilibrium denaturation temperature, Td, defined by DSC, largely unaltered. At pH 4.5−5.0, for example, dgPhy aggregated ∼200 times faster than Phy, even though the difference in Td was only 1−3 °C. To elucidate the mechanism by which the glycans promote kinetic stability, we measured the effect of ionic strength and temperature on the aggregation rate. Also, the second virial coefficients (B22) for the two forms were measured by SLS. These results showed that the aggregation rate of Phy scaled with the concentration of thermally denatured protein. This suggested first-order kinetics with respect to the concentration of the thermally denatured state. A similar but less pronounced correlation was found for dgPhy, and it was suggested that while the aggregation process for the deglycosylated form is dominated by denatured protein, it also involves a smaller contribution from associating molecules in the native state. The measurements of B22 revealed that dgPhy had slightly higher values than Phy. This suggests that dgPhy interacts more favorably with the buffer than Phy and hence rules out strong hydration of the glycans as the origin of their effect on the kinetic stability. On the basis of this and the effects of pH and ionic strength, we suggest that the inhibition of aggregation is more likely to depend on steric hindrance of the glycans in the aggregated form of the protein." @default.
• W2079776446 created "2016-06-24" @default.
• W2079776446 creator A5017699427 @default.
• W2079776446 creator A5027674552 @default.
• W2079776446 creator A5061128509 @default.
• W2079776446 creator A5069236110 @default.
• W2079776446 date "2006-03-24" @default.
• W2079776446 modified "2023-10-16" @default.
• W2079776446 title "Interrelationships of Glycosylation and Aggregation Kinetics for <i>Peniophora lycii </i>Phytase" @default.
• W2079776446 cites W1967733770 @default.
• W2079776446 cites W1982329305 @default.
• W2079776446 cites W1984869639 @default.
• W2079776446 cites W1986741703 @default.
• W2079776446 cites W1999301091 @default.
• W2079776446 cites W2002133276 @default.
• W2079776446 cites W2046029094 @default.
• W2079776446 cites W2051419400 @default.
• W2079776446 cites W2100701404 @default.
• W2079776446 cites W2123331319 @default.
• W2079776446 cites W2125016536 @default.
• W2079776446 cites W2128735483 @default.
• W2079776446 cites W2135964386 @default.
• W2079776446 cites W2150440921 @default.
• W2079776446 cites W2329952272 @default.
• W2079776446 cites W4236190433 @default.
• W2079776446 doi "https://doi.org/10.1021/bi0522955" @default.
• W2079776446 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16605274" @default.
• W2079776446 hasPublicationYear "2006" @default.
• W2079776446 type Work @default.
• W2079776446 sameAs 2079776446 @default.
• W2079776446 citedByCount "41" @default.
• W2079776446 countsByYear W20797764462012 @default.
• W2079776446 countsByYear W20797764462014 @default.
• W2079776446 countsByYear W20797764462016 @default.
• W2079776446 countsByYear W20797764462017 @default.
• W2079776446 countsByYear W20797764462018 @default.
• W2079776446 countsByYear W20797764462019 @default.
• W2079776446 countsByYear W20797764462020 @default.
• W2079776446 countsByYear W20797764462021 @default.
• W2079776446 countsByYear W20797764462023 @default.
• W2079776446 crossrefType "journal-article" @default.
• W2079776446 hasAuthorship W2079776446A5017699427 @default.
• W2079776446 hasAuthorship W2079776446A5027674552 @default.
• W2079776446 hasAuthorship W2079776446A5061128509 @default.
• W2079776446 hasAuthorship W2079776446A5069236110 @default.
• W2079776446 hasConcept C121332964 @default.
• W2079776446 hasConcept C12554922 @default.
• W2079776446 hasConcept C127413603 @default.
• W2079776446 hasConcept C136238340 @default.
• W2079776446 hasConcept C13965031 @default.
• W2079776446 hasConcept C14631669 @default.
• W2079776446 hasConcept C147789679 @default.
• W2079776446 hasConcept C148898269 @default.
• W2079776446 hasConcept C155672457 @default.
• W2079776446 hasConcept C178790620 @default.
• W2079776446 hasConcept C184651966 @default.
• W2079776446 hasConcept C185592680 @default.
• W2079776446 hasConcept C187428577 @default.
• W2079776446 hasConcept C2776923230 @default.
• W2079776446 hasConcept C2777313579 @default.
• W2079776446 hasConcept C42360764 @default.
• W2079776446 hasConcept C55493867 @default.
• W2079776446 hasConcept C59061564 @default.
• W2079776446 hasConcept C62520636 @default.
• W2079776446 hasConcept C86803240 @default.
• W2079776446 hasConceptScore W2079776446C121332964 @default.
• W2079776446 hasConceptScore W2079776446C12554922 @default.
• W2079776446 hasConceptScore W2079776446C127413603 @default.
• W2079776446 hasConceptScore W2079776446C136238340 @default.
• W2079776446 hasConceptScore W2079776446C13965031 @default.
• W2079776446 hasConceptScore W2079776446C14631669 @default.
• W2079776446 hasConceptScore W2079776446C147789679 @default.
• W2079776446 hasConceptScore W2079776446C148898269 @default.
• W2079776446 hasConceptScore W2079776446C155672457 @default.
• W2079776446 hasConceptScore W2079776446C178790620 @default.
• W2079776446 hasConceptScore W2079776446C184651966 @default.
• W2079776446 hasConceptScore W2079776446C185592680 @default.
• W2079776446 hasConceptScore W2079776446C187428577 @default.
• W2079776446 hasConceptScore W2079776446C2776923230 @default.
• W2079776446 hasConceptScore W2079776446C2777313579 @default.
• W2079776446 hasConceptScore W2079776446C42360764 @default.
• W2079776446 hasConceptScore W2079776446C55493867 @default.
• W2079776446 hasConceptScore W2079776446C59061564 @default.
• W2079776446 hasConceptScore W2079776446C62520636 @default.
• W2079776446 hasConceptScore W2079776446C86803240 @default.
• W2079776446 hasIssue "15" @default.
• W2079776446 hasLocation W20797764461 @default.
• W2079776446 hasLocation W20797764462 @default.
• W2079776446 hasOpenAccess W2079776446 @default.
• W2079776446 hasPrimaryLocation W20797764461 @default.
• W2079776446 hasRelatedWork W1799665405 @default.
• W2079776446 hasRelatedWork W1991240338 @default.
• W2079776446 hasRelatedWork W2106601030 @default.
• W2079776446 hasRelatedWork W2348408392 @default.
• W2079776446 hasRelatedWork W2412951868 @default.
• W2079776446 hasRelatedWork W2998950595 @default.
• W2079776446 hasRelatedWork W4211257278 @default.
• W2079776446 hasRelatedWork W422357169 @default.

• next