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1、/.Biockem.99,1147-1155(1986)PurificationandCharacterizationofProteinaseInhibitorsfromWingedBean{Psophocarpustetragonolobiis(L.)DC.)Seeds1HiroshiSH1BATA,*SaburoHARA,*>2TokujiIKENAKA,*andJiroABE**Downloadedfrom*DepartmentofChemistry,OsakaUniversityCollegeofScience,Toyonaka,Osaka560,and**TohokuNat
2、ionalAgriculturalExperimentalStation,Morioka,Iwate020-01Receivedforpublication,November25,1985http://jb.oxfordjournals.org/Sevenproteinaseinhibitorswereisolatedfromwingedbeanseedsbyion-exchangechromatographies.Theseinhibitorshadmolecularweightsofaround20,000,includedfourhalf-cystineresidues,and
3、wereKunitz-typeinhibitors.Two(WTI-2and3)inhibitedbovinetrypsinstronglyandfour(WCI-1,2,3,and4)inhibitedbovinea-chymotrypsin,butindifferentways.OnemoleofWCI-2or-3couldatJohnsHopkinsUniversityonAugust29,2013inhibit2molofa-chymotrypsin.Theremaininginhibitor(WTCI-1)couldbindbothbovinetrypsinanda-chy
4、motrypsinatthemolarratioof1:1,butnotsimul-taneously.Allfourchymotrypsininhibitorscross-reactedwithrabbitanti-WCI-3serum,whiletheotherinhibitorsdidnot.ThemanyproteinproteinaseinhibitorshavebeenKunitz-typeinhibitorshavemolecularweightsofisolatedfromlegumeseedsandcanbeclassifiedaround20,000andincl
5、udetwodisulfidebridges.asBowman-Birk-typeinhibitorsorKunitz-typeTheyhavebeenisolatedfromsoybean(2,3),silkinhibitors.Theformerhavemolecularweightsoftree(4),wingedbean(5-7),Acaciaelata(8),andaround8,000andahighcystinecontent(sevenErythrinalatissima(9).Completeaminoacidse-disulfidebridges),andthei
6、rprimarystructuresandquencesareknownforsoybeantrypsininhibitorsmolecularevolutionhavebeenelucidated(7).(5,10)andwingedbeantrypsininhibitors(7).MoresequencesofKunitz-typeinhibitorsare1ThisworkwassupportedinpartbyaGrant-in-AidforneededfortheinvestigationofmolecularevolutionScientificResearchfromt
7、heMinistryofEducation,andthereactionmechanismsoflegumeseedin-ScienceandCultureofJapan.hibitors.Forthatpurpose,weintendedtopurify2Towhomcorrespondenceshouldbeaddressed.theKunitz-typeinhibitorsfromwingedbeanseeds.Abbreviations:BAEE,