Megazyme/CM Pachyman/P-CMPAC/4克
商品编号：
P-CMPAC
品牌：
Megazyme INC
市场价：
¥3288.00
美元价：
1972.80
产品分类：
其他试剂
公司分类：
Other_reagents
联系Q Q：
3392242852
电话号码：
4000-520-616
电子邮箱：
info@ebiomall.com
商品介绍
HighpurityCM-Pachymanforuseinresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Carboxymethylated,(DS~0.2)highlypurifiedpachyman.Asoluble/gelatinoussubstratefortheassayofendo-1,3-β-D-glucanase.
Identificationofnovelβ-mannan-andβ-glucan-bindingmodules:evidenceforasuperfamilyofcarbohydrate-bindingmodules.
Sunna,A.,Gibbs,M.D.&Bergquist,P.L.(2001).Biochem.J,356(3),791-798.
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Manyglycosidehydrolases,whichdegradelong-chaincarbohydratepolymers,possessdistinctcatalyticmodulesandnon-catalyticcarbohydrate-bindingmodules(CBMs).Onthebasisofconservedproteinsecondarystructure,wedescribeheretheidentificationandexperimentalcharacterizationofnoveltypeofmannanase-associatedmannan-bindingmoduleandalsocharacterizationoftwoCBMfamily4laminarinase-associatedβ-glucan-bindingmodules.ThesemodulesarepredictedtobelongtoasuperfamilyofCBMswhichincludefamilies4,16,17,22andaproposednewfamily,family27.
Lentinulaedodestlg1encodesathaumatin-likeproteinthatisinvolvedinlentinandegradationandfruitingbodysenescence.
Sakamoto,Y.,Watanabe,H.,Nagai,M.,Nakade,K.,Takahashi,M.&Sato,T.(2006).PlantPhysiology,141(2),793-801.
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LentinanisanantitumorproductthatispurifiedfromfreshLentinulaedodesfruitingbodies.Itisacellwallcomponent,comprisingβ-1,3-glucanwithβ-1,6-linkedbranches,whichbecomesdegradedduringpostharvestpreservationasaresultofincreasedglucanaseactivity.Inthisstudy,weusedN-terminalaminoacidsequencetoisolatetlg1,ageneencodingathaumatin-like(TL)proteininL.edodes.TheCDNAclonewasapproximately1.0kbwhereasthegenomicsequencewas2.1kb,andcomparisonofthetwoindicatedthattlg1contains12introns.Thetlg1geneproduct(TLG1)waspredictedtocomprise240aminoacids,withamolecularmassof25kDandisoelectricpointvalueof3.5.Theputativeaminoacidsequenceexhibitsapproximately40%identitywithplantTLproteins,andafungalgenomedatabasesearchrevealedthattheseTLproteinsareconservedinmanyfungiincludingthebasidiomycotaandascomycota.Transcriptionoftlg1wasnotdetectedinvegetativemyceliumoryoungandfreshmushrooms.However,transcriptionincreasedfollowingharvest.Western-blotanalysisdemonstratedariseinTLG1levelsfollowingharvestandsporediffusion.TLG1expressedinEscherichiacoliandAspergillusoryzaeexhibitedβ-1,3-glucanaseactivityand,whenpurifiedfromtheL.edodesfruitingbody,demonstratedlentinandegrADIngactivity.Thus,wesuggestthatTLG1isinvolvedinlentinanandcellwalldegradationduringsenescencefollowingharvestandsporediffusion.
Biochemical,molecularandstructuralanalysisofmultiplethaumatin-likeproteinsfromtheelderberrytree(SambucusnigraL.).
VanDamme,E.J.,Charels,D.,Menu-Bouaouiche,L.,Proost,P.,Barre,A.,Rougé,P.&Peumans,W.J.(2002).Planta,214(6),853-862.
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Thaumatin-likeproteins(TLPs)wereisolatedandcharacterizedfromfruitsandleavesofelderberry(Sambucusnigra)andtheircorrespondinggenescloned.Inaddition,thedevelopmentalregulationandinductionofthedifferentTLPswasfollowedinsomedetail.Ripeningberriesaccumulatedafruit-specificTLPduringthefinalstagesofmaturation.Thisfruit-specificTLPhadnoantifungalactivityandwasdevoidofβ-glucanaseactivity.LeavesconstitutivelyexpressedaTLPthatcloselyresembledthefruit-specifichomologue.TreatmentwithjasmonatemethylesterinducedtwoadditionalTLPsinleavesbutdidnotinduceorenhancetheexpressionofTLPsinimmatureberries.Incontrasttojasmonatemethylester,bothethephonandgarlicextractinducedtheexpressionofaTLPinunripeberriesthatnormallydonotexpressanyTLP.Sequenceanalysisandmolecularmodellingindicatedthatallelderberrythaumatin-likeproteinsshareahighsequencesimilaritywithgroup-5pathogenesis-relatedproteins.However,theproteinsencodedbythedifferentsequencesdifferedfromeachotherinisoelectricpointandthedistributionofthechargesonthesurfaceofthemolecule.
Amolecularbasisfortheendo-β1,3-glucanaseactivityofthethaumatin-likeproteinsfromedIBLefruits.
Menu-Bouaouiche,L.,Vriet,C.,Peumans,W.J.,Barre,A.,VanDamme,E.J.M.&Rougé,P.(2003).Biochimie,85(1),123-131.
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Fruit-specificthaumatin-likeproteinswereisolatedfromcherry,appleandbanana,andtheirenzymaticandantifungalactivitiescompared.Boththeappleandcherrypossessamoderateendo-β1,3-glucanaseactivitybutaredevoidofantifugalactivity.Incontrast,thebananathaumatin-likeproteininhibitstheinvitrohyphalgrowthofVerticilliumalbo-atrumbutisvirtuallydevoidofendo-β1,3-glucanaseactivity.Bothstructuralandmolecularmodelingstudiesshowedthatallthreethaumatin-likeproteinspossessanextendedelectronegativelychargedcleftattheirsurface,whichisbelievedtobeaprerequisiteforendo-β1,3-glucanaseactivity.Dockingexperimentsshowedthatthepositioningoflinear(1,3)-β-D-glucansinthecleftoftheappleandcherryproteinsallowsaninteractionwiththeglutamicacidresiduesthatareresponsibleforthehydrolyticcleavageoftheglucan.Duetoadifferentpositioninginthecleftofthebananathaumatin-likeprotein,thelinearβ-glucanscannotproperlyinteractwiththecatalyticglutamicacidresiduesandasaresulttheproteinpossessesnoenzymaticactivity.Thepossiblefunctionofthefruit-specificthaumatin-likeproteinsisdiscussedinviewoftheobservedBIOLOGicalactivitiesandstructuralfeatures.
Somethaumatin‐likeproteinshydrolysepolymericβ‐1,3‐glucans.
Grenier,J.,Potvin,C.,Trudel,J.&Asselin,A.(1999).ThePlantJournal,19(4),473-480.
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Thaumatinand12purifiedthaumatin-like(TL)proteinsweresurveyedfortheircapacitytohydrolyseβ-1,3-glucansbyusinganin-gelglucanaseassay.SixTLproteinsidentifiedbyN-terminalaminoacidmicrosequencingwerefoundtobeactiveoncarboxymethyl(CM)-pachyman:abarleyleafstress-relatedpermatin,twotomatofruitosmotins,acherryfruitandtwotobaccostigmaproteins.TLenzymesrangedinspecificactivityfrom0.07to89nkatmg-1withCM-pachymanassubstrate.HydrolyticactivitieswerenotrestrictedtoTLproteinsstronglybindingtowater-insolubleβ-1,3-glucanssincethetwoosmotinswereactivewithouttightbindingtopachyman.SomeTLproteinshydrolysedcrudefungalwallsandonebarleyTLenzymeevenlysedfungalspores.Noactivitywasobservedonlaminarininthein-gelhydrolaseassay.Thin-layerchromatographyrevealedthatthesixenzymesactedasendo-β-1,3-glucanasesleadingtotheformationofvariousoligoglucosides.Thusfar,theTLenzymes(EC3.2.1.x)appeareddifferentfromthewell-knownβ-1,3-glucanases(EC3.2.1.39).Noactivitywasfoundwiththaumatin,zeamatin,tobaccoleafPR-Rproteinandfourstress-relatedTLproteinsfrombarleyandpea.ThisisthefirstdemonstrationthatdiverseTLproteinsareenzymaticallyactive.ThefunctionsofsomeTLproteinsmustbereassessedbecausetheydisplayendo-β-1,3-glucanaseactivityonpolymericβ-1,3-glucans.
Characterizationofpeachthaumatin‐likeproteinsandtheiridentificationasmajorpeachallergens.
Palacin,A.,Tordesillas,L.,Gamboa,P.,Sanchez‐Monge,R.,Cuesta‐Herranz,J.,Sanz,M.L.,Barber,D.,SalcedoG.&Díaz‐Perales,A.(2010).Clinical&ExperimentalAllergy,40(9),1422-1430.
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BackgroundPeachisthemostimportantfruitrelatedtofoodallergyintheMediterraneanarea.Prup3,itslipidtransferprotein,hasbeendescribedastheprincipalallergenresponsibleforcross-reactivitieswithotherfoodsandpollenandtheseverityofclinicalsymptoms.However,theinvolvementofotherallergenicfamiliescannotberuledout.Thaumatin-likeproteins(TLPs)havebeendescribedasfoodallergeninseveralfruits,suchasapple,cherry,kiwiandbanana,andpollen.ObjectiveToidentifymembersoftheTLPfamilyinpeachfruitandtocharacterizeputativeallergens.MethodsThroughtwo-dimensional(2D)electrophoresisofpeachextractandimmunodetectionswithapoolofpeach-allergicpatients,IgE-bindingspotswereidentifiedandthecorrespondingproteinspurifiedandcharacterizedasallergensbyinvitroandinvivoassays.Threeisoforms,belongingtotheTLPfamily,werepurifiedbydifferentchromatographicsystemsandcharacterizedbyN-terminalaminoacidsequences,molecularweightdetermination(MALDI)andenzymaticactivityanalysis(β-1,3-gluconasetestandinhibitiongrowthoffungi).Inthesameway,theirIgE-bindingcapacityandallergenicactivityweretestedbyELISAassays,basophilactivationtestsandskinpricktests(SPT).ResultsTwopeach-TLPs,Prup2.0101andPrup2.0201,wereidentifiedasIgE-bindingspotsby2Delectrophoresis.Anotherpeach-TLP,Prup2.0301,wasclonedandproducedasrecombinantproteininayeastsystem.ThethreeisoformswerepurifiedandcharacterizedasTLPsbyimmunoblottingwithanti-chestnutTLPantibodiesandanti-plantN-asparaginecomplexglycan(anti-cross-reactivecarbohydratedeterminant).Allofthemshowedβ-1,3-glucanaseactivityandinhibitionoffungalgrowth.ThethreeTLPswererecognizedbyaround50%oftheserafrom31patientsanalysedinELISAexperiments.AllthreegaveapositiveresponsetoanSPTand/orinbasophilactivationexperiments.ConclusionThreeisoforms,belongingtotheTLPfamily,wereidentifiedinpeachasprincipalallergens.Theirprevalence,observedininvitro,exvivoandinvivoanalyses,suggeststhattheyareimportantallergensandshouldthereforebeincludedintheroutinediagnosisofpeachallergy,atleastintheMediterraneanarea.
Endo-β-1,3-glucanaseGLU1,fromthefruitingbodyofLentinulaedodes,belongstoanewglycosidehydrolasefamily.
Sakamoto,Y.,Nakade,K.&Konno,N.(2011).AppliedandEnvironmentalMicrobiology,77(23),8350-8354.
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ThecellwallofthefruitingbodyofthemushroomLentinulaedodesisdegradedafterharvestingbyenzymessuchasβ-1,3-glucanase.Inthisstudy,anovelendo-typeβ-1,3-glucanase,GLU1,waspurifiedfromL.edodesfruitingbodiesafterharvesting.Thegeneencodingit,glu1,wasisolatedbyrapidamplificationofcDNAends(RACE)-PCRusingprimersdesignedfromtheN-terminalaminoacidsequenceofGLU1.Theputativeaminoacidsequenceofthematureproteincontained247aminoacidresidueswithamolecularmassof26kDaandapIof3.87,andrecombinantGLU1expressedinPichiapastorisexhibitedβ-1,3-glucanaseactivity.GLU1catalyzeddepolymerizationofglucanscomposedofβ-1,3-linkedmainchains,andreactionproductanalysisbythin-layerchromatography(TLC)clearlyindicatedthattheenzymehadanendolyticmode.However,theaminoacidsequenceofGLU1showednosignificantsimilaritytoknownglycosidehydrolases.GLU1hassimilaritytoseveralhypotheticalproteinsinfungi,andGLU1andhighlysimilarproteinsshouldbeclassifiedasanovelglycosidehydrolasefamily(GH128).
Identification,cloning,andcharacterizationofβ-glucosidasefromUstilagoesculenta.
Nakajima,M.,Yamashita,T.,Takahashi,M.,Nakano,Y.&Takeda,T.(2012).AppliedMicrobiologyandBiotechnology,93(5),1989-1998.
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HydrolyticenzymesresponsibleforlaminarindegradationwerefoundtobesecretedduringgrowthofUstilagoesculentaonlaminarin.Anenzymeinvolvedinlaminarindegradationwaspurifiedbyassayingreleaseofglucosefromlaminaribiose.Ion-exchangechromatographyoftheculturefiltratefollowedbysize-exclusionchromatographyyieldeda110-kDaproteinassociatedwithlaminaribiosehydrolysis.LC/MS/MSanalysisofthe110-kDaproteinidentifiedthreepeptidesequencesthatsharedsignificantsimilaritywithaputativeglucosidehydrolasefamily(GH)3β-glucosidaseinUstilagomaydis.BasedontheDNAsequenceoftheU.maydisGH3β-glucosidase,ageneencodingaputativeGH3β-glucosidaseinU.esculenta(Uebgl3A)wasclonedbyPCR.Basedonthededucedaminoacidsequence,theproteinencodedbyUebgl3Ahasamolecularmassof91kDaandshares90%identitywithU.maydisGH3β-glucosidase.RecombinantUeBgl3AexpressedinAspergillusoryzaereleasedglucosefromβ-1,3-,β-1,4-,andβ-1,6-linkedoligosaccharides,andfrom1,3-1,4-β-glucanandlaminarinpolysaccharides,indicatingthatUeBgl3Aisaβ-glucosidase.KineticanalysisshowedthatUeBgl3Apreferentiallyhydrolyzedlaminaritrioseandlaminaritetraose.TheseresultssuggestthatUeBgl3AisakeyenzymethatproducesglucosefromlaminarioligosaccharidesduringgrowthofU.esculentaonlaminarin.
Detectionofenzymesactiveonvariousβ‐1,3‐glucansafterdenaturingpolyacrylamidegelelectrophoresis.
Trudel,J.,Grenier,J.&Asselin,A.(1998).Electrophoresis,19(10),1788-1792.
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Enzymeswereassayedforglucanaseactivityafterdenaturingsodiumdodecylsulfate-polyacrylamidegelelectrophoresis(SDS-PAGE)ingelscontainingβ-1,3-glucansembeddedassubstrate.Lentinan,curdlan,paramylon,baker"syeastalkali-insolubleglucan,baker"syeastalkali-solubleglucanandcarboxymethyl(CM)-pachymanwerecomparedtooligomericlaminarin,whichistheusualsubstrateforassayingβ-1,3-glucanaseactivities.Detectingenzymeactivitiesbyanilinebluefluorescentstainingwasalsocomparedwiththestainingofreleasedreducingsugarsby2,3,5-triphenyltetrazoliumchloride(TTC).Forthenonreducedproteins,theDriselaseextractexhibitedonemajorbandat32.5kDaandonelessintensebandat23kDaformostsubstrateswiththetwodetectionprocedures.NoLyticaseenzymewasdetectedineitherdetectionproceduresforalltestedsubstrates.Forbarleyenzymes,noactivitywasrevealedafteranilinebluestainingwhileoneundescribed19kDaglucanaseactivitywasbestshownafterTTCstainingwithcurdlan,paramylonandCM-pachymanassubstrates.Inthecaseofreducedproteins,theLyticaseextractyieldedthreebands(33,36and46kDa)onseveralsubstrateswithbothdetectionprocedures.Thiswasthesameforthebarleyleafextract(32,36and39kDa).TheDriselaseextractshowedone42kDaband.Manyenzymesactiveonβ-1,3-glucansarethusbestrevealedwhenproteinsaredenaturedandreducedandwhenproteinrenaturationafterSDS-PAGEinvolvesapH8.0treatmentandtheinclusionof1mMcysteineinbuffers.However,someenzymesareonlydetectedwhenproteinsaredenaturedwithoutreduction.Finally,theuseofvariouspolymericβ-1,3-glucansubstratesdifferentfromoligomericlaminarinisnecessarytodetectnewtypesofenzymessuchasthe19kDabarleyglucanase.
Developmentofβ‐1,3‐glucanaseactivityingerminatedtomatoseeds.
Morohashi,Y.&Matsushima,H.(2000).JournalofExperimentalBotany,51(349),1381-1387.
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Laminarin‐hydrolysingactivitydevelopedintheendospermoftomato(Lycopersiconesculentum)seedsfollowinggermination.Theenzymewasbasic(pI>10)andtheapparentmolecularmasswasestimatedtobe35 kDabySDS‐PAGE.Itwasspecificforlinearβ‐1,3‐glucansubstrates.Laminarinwashydrolysedbytheenzymetoyieldamixtureofoligoglucosides,indicatingthattheenzymehadanendo‐actionpattern.Thus,theenzymewasidentifiedasβ‐1,3‐endoglucanase(EC3.2.1.39).Theactivityoftheenzymedevelopedintheendospermafterradicleprotrusion(germination)hadoccurredandtheenzymeactivitywaslocalizedexclusivelyinthemicropylarregionoftheendospermwheretheradiclehadpenetrated.Whenthelateralendospermregion,wherenoinductionoftheenzymeoccurred,waswounded(cutorpunctured),therewasamarkedenhancementofβ‐1,3‐glucanaseactivity.Thusthepost‐germinativeβ‐1,3‐glucanaseactivityinthemicropylarendospermportionmightbebroughtaboutbywoundingresultingfromendospermrupturebyradiclepenetration.
品牌介绍
Megazyme品牌产品简介
来源：作者：人气：2149发表时间：2016-05-19 10:59:00【大 中 小】
Megazyme是一家全球性公司，专注于开发和提供用于饮料、谷物、乳制品、食品、饲料、发酵、生物燃料和葡萄酒产业用的分析试剂、酶和检测试剂盒。Megazyme的许多检测试剂盒产品已经为众多官方科学协会（包括AOAC, AACC , RACI, EBC和ICC等），经过严格的审核，批准认证为官方标准方法，确保以准确、可靠、定量和易于使用的测试方法，满足客户的质量诉求。
Megazyme的主要产品线包括：
◆ 检测试剂盒
◆ 酶
◆ 酶底物
◆ 碳水化合物
◆ 化学品/仪器
官网地址：http://www.megazyme.com
检测试剂盒特色产品：
货号
中文品名
用途
K-ACETAF
乙酸[AF法]检测试剂盒
酶法定量分析乙酸最广泛使用的方法
K-ACHDF
可吸收糖/膳食纤维检测试剂盒
酒精沉淀法测定膳食纤维
K-AMIAR
氨快速检测试剂盒
用于包括葡萄汁、葡萄酒以及其它食品饮料样品中氨含量的快速检测分析。
K-AMYL
直链淀粉/支链淀粉检测试剂盒
谷物淀粉和而粉中直链淀粉/支链淀粉比例和含量检测
K-ARAB
阿拉伯聚糖检测试剂盒
果汁浓缩液中阿拉伯聚糖的检测
K-ASNAM
L-天冬酰胺/L-谷氨酰胺和氨快速检测试剂盒
用于食品工业中丙烯酰胺前体、细胞培养基、以及上清液组分中、L-天冬酰胺，谷氨酰胺和氨的检测分析
K-ASPTM
阿斯巴甜检测试剂盒
专业用于测定饮料和食品中阿斯巴甜含量，操作简单
K-BETA3
β-淀粉酶检测试剂盒
适用于麦芽粉中β-淀粉酶的测定
K-BGLU
混合键β-葡聚糖检测试剂盒
测定谷物、荞麦粉、麦汁、啤酒及其它食品中混合键β-葡聚糖(1,3:1,4-β-D-葡聚糖)的含量
K-CERA
α-淀粉酶检测试剂盒
谷物和发酵液（真菌和细菌）中α-淀粉酶的分析测定
K-CITR
柠檬酸检测试剂盒
快速、可靠地检测食品、饮料和其它物料中柠檬酸（柠檬酸盐）含量
K-DLATE
乳酸快速检测试剂盒
快速、特异性检测饮料、肉类、奶制品和其它食品中L-乳酸和D-乳酸(乳酸盐）含量
K-EBHLG
酵母β-葡聚糖酶检测试剂盒
用于测量和分析酵母中1,3:1,6?-β-葡聚糖，也可以检测1,3-葡聚糖
K-ETSULPH
总亚硫酸检测试剂盒
测定葡萄酒、饮料、食品和其他物料中总亚硫酸含量（按二氧化硫计）的一种简单，高效，可靠的酶法检测方法
K-FRGLMQ
D-果糖/D-葡萄糖[MegaQuant法]检测试剂盒
适用于使用megaquant?色度计（505nm下）测定葡萄、葡萄汁和葡萄酒中D-果糖和D-葡萄糖的含量。
K-FRUC
果聚糖检测试剂盒
含有淀粉、蔗糖和其他糖类的植物提取物和食品中果聚糖的含量测定。
K-FRUGL
D-果糖/D-葡萄糖检测试剂盒
对植物和食品中果糖或葡萄糖含量的酶法紫外分光测定。
K-GALM
半乳甘露聚糖检测试剂盒
食品和植物产品中半乳甘露聚糖的含量检测
K-GLUC
D-葡萄糖[GOPOD]检测试剂盒
谷物提取物中D-葡萄糖的含量测定，可以和其它Megazyme检测试剂盒联合使用。
K-GLUHK
D-葡萄糖[HK]检测试剂盒
植物和食品中D-葡萄糖的含量测定，可以和其它Megazyme检测试剂盒联合使用。
K-GLUM
葡甘聚糖检测试剂盒
植物和食品中葡甘聚糖的含量测定。
K-INTDF
总膳食纤维检测试剂盒
总膳食纤维特定检测和分析
K-LACGAR
乳糖/D-半乳糖快速检测试剂盒
用于快速检测食品和植物产品中乳糖、D-半乳糖和L-阿拉伯糖
K-LACSU
乳糖/蔗糖/D-葡萄糖检测试剂盒
混合面粉和其它物料中蔗糖、乳糖和D-葡萄糖的测定
K-LACTUL
乳果糖检测试剂盒
特异性、快速和灵敏测量奶基样品中乳果糖含量
K-MANGL
D-甘露糖/D-果糖/D-葡萄糖检测试剂盒
适合测定植物产品和多糖酸性水解产物中D-甘露糖含量
K-MASUG
麦芽糖/蔗糖/D-葡萄糖检测试剂盒
在植物和食品中麦芽糖，蔗糖和葡萄糖的含量检测
K-PECID
胶质识别检测试剂盒
食品配料中果胶的鉴别
K-PHYT
植酸(总磷)检测试剂盒
食品和饲料样品植酸/总磷含量测量的简便方法。不需要通过阴离子交换色谱对植酸纯化，适合于大量样本分析
K-PYRUV
丙酮酸检测试剂盒
在啤酒、葡萄酒、果汁、食品和体液中丙酮酸分析
K-RAFGA
棉子糖/D-半乳糖检测试剂盒
快速测量植物材料和食品中棉子糖和半乳糖含量
K-RAFGL
棉子糖/蔗糖/D-半乳糖检测试剂盒
分析种子和种子粉中D-葡萄糖、蔗糖、棉子糖、水苏糖和毛蕊花糖含量。通过将棉子糖、水苏糖和毛蕊花糖酶解D-葡萄糖、D-果糖和半乳糖，从而测定葡萄糖含量来确定
K-SDAM
淀粉损伤检测试剂盒
谷物面粉中淀粉损伤的检测和分析
K-SUCGL
蔗糖/D-葡萄糖检测试剂盒
饮料、果汁、蜂蜜和食品中蔗糖和葡萄糖的分析
K-SUFRG
蔗糖/D-果糖/D-葡萄糖检测试剂盒
适用于植物和食品中蔗糖、D-葡萄糖和D-果糖的测定
K-TDFR
总膳食纤维检测试剂盒
总膳食纤维检测
K-TREH
海藻糖检测试剂盒
快速、可靠地检测食品、饮料和其它物料中海藻糖含量
K-URAMR
尿素/氨快速检测试剂盒
适用于水、饮料、乳制品和食品中尿素和氨的快速测定
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