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ProteinScience(1992),I,120-131.CambridgeUniversityPress.PrintedintheUSA.
Copyright01992TheProteinSociety0961-8368/92$5.00+.OO
Stability,quaternarystructure,andfoldingof
internal,external,andcore-glycosylated
invertasefromyeast
GUNTHERKERN,NORBERTSCHULKE,FRANZX.SCHMID,*
ANDRAINERJAENICKE
lnstitutfurBiophysikundPhysikalischeBiochemie,UniversitatRegensburg,D-8400Regensburg,Germany
*LaboratoriumfurBiochemie,UniversitatBayreuth,D-8580Bayreuth,Germany
(RECEIVEDAugust22,1991;ACCEPTEDSeptember5,1991)
Abstract
Theroleofcarbohydratechainsforthestructure,function,stability,andfoldingofglycoproteinshasbeen
investigatedusinginvertaseasamodel.Theproteinisencodedbyseveraldifferentgenes,anditscarbohydrate
moietyisheterogeneous.Bothpropertiescomplicatephysicochemicalcomparisons.Hereweusedthetemperature-
sensitivesecl8secretionmutantofyeastwithasingleinvertasegene(SUC2).Thismutantproducesthe
carbohydrate-freeinternalinvertase,thecore-glycosylatedform,and,atthepermissivetemperature,thefully
glycosylatedexternalenzyme,allwithidenticalproteinmoieties.Thecore-glycosylatedenzymeresemblesthenas-
centglycoproteinchainthatfoldsintheendoplasmicreticulum.Therefore,itmaybeconsideredamodelforthe
invivofoldingofglycoproteins.Inaddition,becauseofitsuniformglycosylation,itcanbeusedtoinvestigate
thestateofassociationofnativeinvertase.
Glycosylationisfoundtostabilizetheproteinwithrespecttothermaldenaturationandchaotropicsolventcom-
ponents;thestabilizingeffectdoesnotdifferfortheexternalandthecore-glycosylatedforms.Unliketheinter-
nalenzyme,theglycosylatedformsareprotectedfromaggregation.
Na
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