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The behavior of R-ovalbumin and its individual components A(1), A(2), and A(3) in urea solution: Kinetics and equilibria

McKenzie, Hugh; Frier, Robert

Description

Procedures are described for the isolation of the individual components A1, A2, and A3 of native R-ovalbumin from freshly laid domestic hen eggs. Because heavy metal ion contaminants result in spurious irreproducible kinetics, particularly at high pH, considerable care is taken to avoid their presence. Kinetics studies are made of the behavior of whole R-ovalbumin and its individual components in urea solution over the pH range 3.7-9.6 following the reaction by determining absorbance...[Show more]

dc.contributor.authorMcKenzie, Hugh
dc.contributor.authorFrier, Robert
dc.date.accessioned2015-12-13T22:37:38Z
dc.date.available2015-12-13T22:37:38Z
dc.identifier.issn0277-8033
dc.identifier.urihttp://hdl.handle.net/1885/77183
dc.description.abstractProcedures are described for the isolation of the individual components A1, A2, and A3 of native R-ovalbumin from freshly laid domestic hen eggs. Because heavy metal ion contaminants result in spurious irreproducible kinetics, particularly at high pH, considerable care is taken to avoid their presence. Kinetics studies are made of the behavior of whole R-ovalbumin and its individual components in urea solution over the pH range 3.7-9.6 following the reaction by determining absorbance differences at 233, 287, and 293 nm and ORD and CD changes at 350 and 221 nm, respectively. Reaction is rapid at low pH, slowing with increasing pH. Except under limited conditions, the reaction is not simple first order. Equations are presented for describing the reactions, and the nature of the reaction products is considered. Unfolding equilibrium profiles were also determined by ORD at several wavelengths and were not stigmoidal in shape and the normalized curves were not superimposed.
dc.publisherKluwer Academic Publishers
dc.sourceJournal of Protein Chemistry
dc.subjectKeywords: ovalbumin; urea; article; conformational transition; equilibrium constant; hen; molecular dynamics; nonhuman; optical rotation; pH; protein folding; protein isolation; Animals; Chickens; Circular Dichroism; Egg White; Kinetics; Optical Rotatory Dispersion Equilibria; Kinetics; R-ovalbumin A1, A2, A3 isolation; Urea unfolding
dc.titleThe behavior of R-ovalbumin and its individual components A(1), A(2), and A(3) in urea solution: Kinetics and equilibria
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume22
dc.date.issued2003
local.identifier.absfor110106 - Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)
local.identifier.ariespublicationMigratedxPub6077
local.type.statusPublished Version
local.contributor.affiliationMcKenzie, Hugh, University of New South Wales, ADFA
local.contributor.affiliationFrier, Robert, College of Medicine, Biology and Environment, ANU
local.bibliographicCitation.issue3
local.bibliographicCitation.startpage207
local.bibliographicCitation.lastpage214
local.identifier.doi10.1023/A:1025076621515
dc.date.updated2015-12-11T09:37:30Z
local.identifier.scopusID2-s2.0-0041353878
CollectionsANU Research Publications

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