Description

CleavesN-linkedglycansfromglycopeptides,includingglycanswithα(1,3)-linkedcorefucoseasseenininsectsandplants. PeptideN-GlycosidaseA,Glycopeptidasefromalmonds,Almondglycoamidase,Peptide-N(4)-(N-acetyl-βglucosaminyl)asparagineamidase.

Source:
Almond.

Specificity:

PNGaseAfromalmondscleavesN-GlycanchainslinkedtoAsparaginefromglycopeptides.TheenzymehydrolyzesanN(4)-(acetyl-βD-glucosaminyl)asparagineresidueinwhichtheglucosamineresiduemaybefurtherglycosylated,toyielda(substituted)N-acetyl-βD-glucosaminylamineandapeptidecontaininganaspartateresidue.

TheenzymecleavesN-glycanswithorwithoutα(1,3)-linkedcorefucoseresiduespresentininsectandplantglycoproteins.ThisdiffersfromPNGaseF,whichcannotremoveN-glycanswithα(1,3)-linkedcorefucose. PNGaseArequiresglycopeptidesassubstrates.Glycopeptidescanbeobtainedbydigestingtheglycoproteinwithtrypsin[1,2]orpepsin.Doesnotacton(GlcNAc)-Asn,becauseitrequiresthepresenceofmorethantwoaminoacidresiduesinthesubstrate.

Shipswith: WS0273 Reactionbuffer:50mMcitrate-phosphatebuffer,pH5.0,0.02%sodiumazide.

Formulation:
Lyophilizedpowdercontainingcitrate-phosphatebuffer,pH5.0.

pHRange:
Optimum:pH5.0Range:pH4.0-6.0

UnitDefinition:
Oneunitisdefinedastheamountofenzymerequiredtohydrolyze1μmolovalbuminglycopeptideperminatpH5.0and37°C.

Size:10mU

ProductCode: GKE-5011B

1. KüsterB,WheelerSF,HunterAP,DwekRA,HarveyDJ. SequencingofN-linkedoligosaccharidesdirectlyfromproteingels:in-geldeglycosylationfollowedbymatrix-assistedlaserdesorption/ionizationmassspectrometryandnormal-phasehigh-performanceliquidchromatography. AnalBiochem.1997Jul15;250(1):82-101.

2. KolarichD,AltmannF. N-Glycananalysisbymatrix-assistedlaserdesorption/ionizationmassspectrometryofelectrophoreticallyseparatednonmammalianproteins:applicationtopeanutallergenArah1andolivepollenallergenOlee1. AnalBiochem.2000Oct1;285(1):64-75.

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