DK150170B - Fremgangsmaade til bestemmelse af et antigen eller dets tilsvarende antistof - Google Patents
Fremgangsmaade til bestemmelse af et antigen eller dets tilsvarende antistof Download PDFInfo
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Description
i 150170
Den foreliggende opfindelse angår en fremgangsmåde til bestemmelse af et antigen eller dets tilsvarende antistof under anvendelse af sådanne komponenters kendte bindingsaffinitet.
5
Til påvisning og bestemmelse af stoffer, der spiller en fremherskende rolle ved biokemiske processer, dvs. lavmolekylære stoffer, såsom vitaminer og steroider, eller højmolekylære stoffer, såsom proteiner og kulhydrater, er det ofte muligt 10 at anvende reaktioner mellem disse stoffer og proteiner med en specifik bindingsaffinitet til disse stoffer. Det er således muligt at bestemme koncentrationen af et steroid ved anvendelse af et protein, der er i stand til at binde dette steroid specifikt. Som eksempler på sådanne kombinationer ^5 kan nævnes cortisol og transcortin, 17/3-østradiol samt det østradiolbindende receptorprotein i uterus.
Det er også muligt at knytte et lavmolekylært stof kemisk til et protein og at injicere dette konjugat i et forsøgs-2Q dyr, som derpå reagerer ved at danne antistoffer mod blandt andre det lavmolekylære stof. Sidstnævnte skal i dette tilfælde betragtes som et såkaldt hapten. Antistofferne mod haptenet kan betragtes som et særtilfælde af specifikke bindingsproteiner.
25 Højmolekylære stoffer, såsom simple og konjugerede proteiner og kulhydrater, er i stand til at forårsage dannelse af antistoffer ved injicering i dyr under de korrekte forsøgsbetingelser. Mellem disse antistoffer og det injicerede højmole-3q kylære stof, antigenet, er der igen tale om specifik bindingsaffinitet.
Påvisningsmetoder, ved hvilke disse specifikke bindingsaffiniteter anvendes, er ofte baseret på konkurrence mellem det 35 stof, der skal bestemmes i prøven, og den kendte mængde af det samme stof, der er radioaktivt mærket, med hensyn til 2 150170 en begrænset mængde af dets bindingspartner. Den stofmængde, der skal bestemmes, bestemmer hvilken del af det radioaktivt mærkede stof, der kan bindes ved hjælp af dens bindingspartner. Det er også muligt at bestemme en ukendt mængde speci-5 fikt bindingsprotein ved omsætning af en prøve deraf med en vis mængde radioaktivt mærket, specifikt bindende stof. De udtryk, hvormed disse metoder betegnes i litteraturen, afhænger af naturen af det specifikke bindingsprotein. Der er tale om "konkurrerende proteinbindingsbestemmelser", hvor re-2o ceptor- eller transportproteiner anvendes, og om "radioimmunologiske bestemmelser", hvor antistoffer anvendes som specifikt bindingsprotein.
I stedet for mærkning af den ene af komponenterne i de oven-25 for beskrevne reaktioner med en radioaktiv isotop, er det også muligt at anvende et enzym som et mærkende stof. Når der gøres brug af bindingsaffiniteten mellem et lavmolekylært stof og dets specifikke bindingsprotein, kan det lavmolekylære stof kobles til et enzym. Koblingsproduktet, dvs.
2o lavmolekylært stof/enzym, kan derpå anvendes ved forsøg som ovenfor beskrevet. Når der gøres brug af bindingsaffiniteten mellem et antigen og dets antistof, kan antigenet eksempelvis kobles til et enzym i stedet for at blive mærket med en radioaktiv isotop, således som det er konventionelt i forbin-25 delse med radioimmunologiske metoder.
Ved alle de metoder, hvor en sådan mærket reaktionskomponent anvendes, er en passende metode til fraskillelse af den frie, mærkede komponent, som er knyttet til bindingspartneren, af 30 afgørende betydning. Afhængigt af naturen af de stoffer, der deltager i reaktionen, kan forskellige separationsmetoder anvendes, f.eks. elektroforese, gelfiltrering, selektiv adsorption, anvendelse af den ene af reaktionskomponenterne i en insolubiliseret form samt anvendelse af antistoffer overfor 35 en' af reaktionskomponenterne, også i en insolubiliseret form.
3 150170 På trods af den høje følsomhed, der kan opnås ved hjælp af disse metoder, er det ikke altid muligt at påvise eller bestemme stoffer, der forekommer i ekstremt lave koncentrationer i eksempelvis serum eller urin. Det er således meget vanske-5 ligt og ofte umuligt at påvise adrenocorticotropt hormon (ACTH) ved hjælp af en radioimmulogisk metode, med mindre man til rådighed har et meget sjældent antiserum indeholdende antistoffer med en ekstremt høj bindingsaffinitet til ACTH.
10 Også bestemmelser af mindre peptidhormoner, såsom oxytocin i ikke-ekstraheret serum, forårsager store vanskeligheder, fordi den krævede følsomhed ikke kan opnås.
Selvom den immunologiske krydsreaktion mellem HCG og LH i 15 princippet muliggør bestemmelse af begge hormoner med et prøvesystem, kan de fleste metoder til bestemmelse af humant chorio-nisk gonadotropin (HCG) ved hjælp af et koblingsprodukt mellem HCG og et enzym ikke anvendes til påvisning og bestemmelse af luteiniserende hormon (LH). Dette skyldes det faktum, at 20 LH forekommer i meget lavere koncentrationer i blod og urin end HCG under graviditet, så at prøvesystemernes følsomhed er utilstrækkelig. Denne mangel på følsomhed kan formindskes ved ekstraktion af stoffet, der skal bestemmes, fra det medium, hvori det forekommer, eller ved at koncentrere mediet.
25 Disse metoder er imidlertid meget arbejdskrævende, og resultaterne er ofte utilfredsstillende.
Der er nu fundet frem til en fremgangsmåde til bestemmelse af en komponent i reaktionen mellem specifikke 30 bindingsproteiner og de stoffer, der kan bindes specifikt ved hjælp af disse proteiner, idet man gør brug af sådanne komponenters kendte bindingsaffinitet til hinanden. Fremgangsmåden ifølge opfindelsen er i overensstemmelse hermed ejendommelig ved, at komponenten, der skal bestemmes, omsættes med 35 sin bindingspartner, som er insolubiliseret eller bliver in-solubiliseret, at den faste fase skilles fra den flydende fase, at den faste fase derpå omsættes med en immunologisk 4 150170 komponent, der er i stand til at reagere med en i den faste fase tilstedeværende komponent, hvorhos den immunologiske komponent er koblet til et enzym, og at den flydende eller faste fases enzymaktivitet til slut bestemmes, hvilken akti-5 vitet er et mål for mængden af det stof, der skal bestemmes.
Bindingspartneren, der kræves til bestemmelse af den i en ukendt mængde foreliggende komponent, anvendes i en uopløselig form. Bestemmelsen kan finde sted ved at sætte bindings-10 partneren til reaktionsblandingen i en uopløselig form og derpå omsætte blandingen i et heterogent medium, men bindings-partneren kan også tilsættes i opløst form, hvorefter den kan insolubiliseres ved tilsætning af antistoffer overfor den.
15
Stoffet, der er i stand til at reagere specifikt med en af reaktionskomponenterne, og som anvendes koblet til et enzym, kan være den anden reaktionskomponent, men kan også være et tredje stof, som skal have en specifik affinitet til en af 2 0 reaktionskomponenterne.
Fremgangsmåden kan anvendes til de forskellige reaktionssystemer, der er beskrevet i det foregående, dvs. antigen/antistof, hapten/antistof og et lavmolekylært stof/specifikt bindings-25 protein. Som tredje stof kan anvendes et andet antistof, dvs. et antistof overfor γ-globulinfraktionen fra den dyreart, i hvilken de første antistoffer er blevet dannet. Denne situation kan forekomme i systemerne antigen/(første) antistof og hapten/(første) antistof. Som tredje stof kan også anven-30 des et antistof overfor et specifikt bindingsprotein.
Kernepunktet i den omhandlede fremgangsmåde er udførelsen i to trin, mellem hvilke en separation finder sted mellem væsken og reaktionsblandingens faste fase. Det andet trin 35 gennemføres med den faste fase. Kun på dette trin anvendes enzymkoblingsproduktet, og enzymaktiviteten bestemmes.
5 150170
De vigtigste fordele ved fremgangsmåden ifølge opfindelsen er: 1) det første trin kan udføres i et større volumen end det 5 er ønskeligt eller muligt for det andet trin. Dette er af stor betydning, når stoffet, der skal bestemmes, forekommer i for lave koncentrationer til at kunne bestemmes ved hjælp af kendte metoder.
10 2) I den væske, der skal undersøges, kan der være stoffer til stede, som påvirker reaktionerne i det andet trin på ugunstig måde. Specielt kan det i koblingsproduktet tilstedeværende enzym samt den enzymatisk katalyserede reaktion være følsomme overfor forstyrrende stoffer i prøvevæsken.
15
Den omhandlede fremgangsmåde kan især anvendes til bestemmelse af stoffer, som findes i legemsvæsker, såsom hormoner, disses antistoffer og specifikke bindingsproteiner samt enzymer.
Også faktorer for blodkoagulation, fibrinolyse og komplement-20 systemer, patologiske proteiner i legemsvæsker samt antistoffer overfor patogene mikroorganismer og iso-antistoffer kan bestemmes på denne måde.
Mediet, hvori bestemmelsens første trin finder sted, består 25 ofte af en stor mængde forsøgsvæske, såsom urin eller serum.
Hvis det anses for nødvendigt, kan mediet indstilles til den til den immunokemiske reaktion nødvendige pH-værdi, nemlig mellem 5 og 9, ved tilsætning af et tørt puffersalt eller et ringe volumen af en koncentreret pufferopløsning. Det an-30 det trins medium er også en puffer med en for den immunokemiske reaktion nødvendig pH-værdi. Til dette formål kan anvendes phosphatpuffere, citratpuffere, tris(hydroxymethyl)-aminomethan samt imidazolpuffere. Det kan være nødvendigt for den pågældende enzymreaktion at anvende en puffer med 35 en anden sammensætning og pH-værdi, som afhænger af det benyttede enzym.
6 150170
Fremstillingen af den insolubiliserede reaktionskomponent kan finde sted på forskellige måder, f.eks. afhængigt af denne reaktionskomponents egenskaber. Antistoffer, specifikke bindingsproteiner og proteinlignende antigen kan således in-5 solubiliseres ved hjælp af tværbinding, f.eks. med glutar-aldehyd og chlormyresyreethylester, ved hjælp af fysisk adsorption eller kemisk kobling til en uopløselig bærer, såsom celluloseforbindelser, agarose, tværbundet dextran, polystyren og lignende, eller ved kobling til antistoffer overfor 10 det pågældende protein, som er koblet til en uopløselig bærer. Lavmolekylære stoffer kan bindes ved hjælp af metoder, der afhænger af opbygningen af det lavmolekylære stof og bærermaterialet. Nogle af de lavmolekylere stoffer kan allerede have grupper, der er i stand til at reagere med de reaktive 15 dele på bsrermaterialet. I andre tilfælde skal sådanne grupper indføres ved hjælp af organisk-kemiske reaktioner.
Fremstillingen af enzymkoblingsprodukterne kan også foretages ved hjælp af metoder, der afhænger af det i koblingsproduk-20 tet inkorporerede molekyles egenskaber. En covalent binding af proteiner til enzymer kan foretages ved hjælp af sådanne reagenser som carbodiimider, diisocyanater, glutaraldehyd og bis-diazobenzidin. Koblingen af lavmolekylære stoffer kan finde sted på forskellige måder. Nogle af disse stoffer kan 25 allerede indeholde grupper, der kan tværbindes med reaktive grupper i enzymet. I andre tilfælde skal sådanne grupper indføres ved hjælp af organisk-kemiske reaktioner. Det vil fremgå , at ved fremstillingen af disse koblingsprodukter må de til enzymet bundne stoffers oprindelige bindingsegenskaber 30 ikke ændres ret meget. Enzymets aktivitet må heller ikke blive formindsket i væsentlig grad.
Valget af enzymet, der skal udgøre en del af koblingsproduktet, bestemmes af sådanne egenskaber som den specifikke bin-35 dingsaktivitet (en høj omdannelseshastighed forøger prøvesystemets følsomhed) og enkelheden ved enzymbestemmelsen. Bestemmelsen af et enzym, som katalyserer en omdannelse, i 7 150170 hvilken farvede reaktionskomponenter deltager/ er enkel. Sådanne kolorimetriske bestemmelser kan automatiseres på enkel måde.
5 Det er også muligt at anvende' enzymer/ der katalyserer'så danne omdannelser, hvori der deltager reaktionskomponenter, som kan bestemmes spektrofotometrisk eller fluorime'trisk.
Disse bestemmelser kan også automatiseres.
10 Ved fremstillingen af koblingsprodukterne foretrækkes sådanne enzymer som katalase, peroxidase, ø-glucuronidase, Ø-B-gluco-sidase, β-D-galactosidase, urease, glucose-oxidase og galac-tose-oxidase, især gruppen af oxidoreduktaser.
15 Bestemmelserne ved fremgangsmåden ifølge opfindelsen foretages i store træk som følger: Et bestemt volumen af en prøvevæske, f.eks. 10 ml, indeholdende en meget lav koncentration af komponenten, der skal bestemmes, blandes med en bestemt mængde af en insolubiliseret reaktionspartner for det stof, som skal 20 bestemmes. Prøvevæsken kan være urin, hvori komponenten, der skal bestemmes, findes i lav koncentration, eller serum, der er blevet fortyndet med henblik på at formindske forstyrrende faktorers indflydelse. For at muliggøre reaktionen, der skal udføres i det heterogene system, omrøres blandingen. Den re-25 suiterende faste fase skilles fra prøvevæsken, f.eks. ved hjælp af centrifugering, og vaskes om nødvendigt. Den første del af bestemmelsen kan også foretages ved inkubation af prøvevæsken med en bestemt mængde af reaktionspartneren for stoffet, der skal bestemmes, i opløst form, hvorefter en mængde insolu-30 biliseret antistof overfor denne reaktionspartner tilsættes, og blandingen omrøres og til slut centrifugeres. Separation ved hjælp af filtrering og dekantering er også mulig.
Den anden del af bestemmelsen gennemføres ved at resuspen-35 dere det uopløselige stof, som danner den faste fase, fortrinsvis i en puffer, og ved at omsætte den med en bestemt mængde af et koblingsprodukt mellem stoffet, der skal bestemmes, 8 150170 og et enzym, f.eks. peroxidase. Efter en bestemt tid fraskilles den faste fase atter, f.eks. ved hjælp af centrifugering, hvorpå enzymaktiviteten i den flydende fase bestemmes. Den-nem enzymaktivitet er et mål for den stofmængde, som skal 5 bestemmes i prøvevæsken. Den anden del af bestemmelsen kan også udføres ved omsætning af det uopløselige stof fra den første del af bestemmelsen med et koblingsprodukt, som er opnået ved at binde et tredje stof, der er i stand til specifikt at reagere med reaktionskomponenten, som skal bestem-10 mes, til et enzym. Dette vil være tilfældet, når et antistof bestemmes ved hjælp af det insolubiliserede tilsvarende antigen i den første del af bestemmelsen, og et andet antistof overfor det første, som er koblet til et enzym, benyttes i den anden del af bestemmelsen.
15
Enzymaktiviteten i en fase af reaktionsblandingen måles ved inkubation af ’denne fase méd et substrat som andre stoffer, der kræves til den pågældende enzymreaktion.
20 Fortrinsvis anvendes en reaktion, ved hvilken en farvet forbindelse dannes eller fjernes, hvis adsorption let kan bestemmes kvantitativt.
Reagenserne kan anvendes i mangfoldige former. Den komponent 25 i reaktionssystemet, der er koblet til et enzym, kan være opløst i en puffer eller være frysetørret. Også en fast bærer kan anvendes, f.eks. en papirstrimmel, der er imprægneret med enzymkoblingsproduktet.
30 Den uopløselige komponent kan forarbejdes til partikler af forskellige størrelser, såsom korn, plader og stænger, eller til en strimmel af et andet bærermateriale.
Til udførelsen af fremgangsmåden ifølge opfindelsen anvendes 35 sædvanligvis en prøvepakke, der hovedsagelig består af: 9 150170 a) en bestemt mængde af enzymkoblingsproduktet, b) en tilsvarende mængde af en af reaktionssystemets komponenter i uopløselig form, og 5 c) et substrat til bestemmelse af den benyttede enzymmængde.
Prøvepakken kan, hvis det er påkrævet, indeholde de ønskede hjælpemidler til fremstilling af en fortyndingsrække af 10 den prøve, der skal undersøges, med henblik på en kvantitativ bestemmelse, såsom prøverør, pipetter og kolber indeholdende et fortyndingsmiddel. Til bestemmelsen af antigener eller haptener eller disses antistoffer indeholder prøvepakken i det mindste: 15 a) en bestemt mængde af koblingsproduktet mellem antigenet haptenet eller et antistof i forhold hertil og et enzym, b) en tilsvarende mængde af en insolubiliseret komponent i 20 reaktionssystemet antigen/antistof eller hapten/antistof, og c) et substrat til bestemmelse af enzymaktiviteten.
Opfindelsen illustreres nærmere i de efterfølgende eksem-25 pier.
Eksempel 1 150170
IQ
Bestemmelse af humant chorionisk gonadotropin (HCG) i serum.
a) Fremstilling af HCG—HEP.
5 mg HCG· og 20 mg peberrod-peroxidase (HEP) blev opløst i 2 ml 0,05 M phosphatpuffer med pH 6,2. Efter tilsætning af 40 μ/1 251 glutaraldéhyd-opløsning blev blandingen rystet ved stuetemperatur i to timer. Derefter blev blandingen centrifugeret i 5 minutter ved 250- g, hvorefter den blev fraktioneret over "Sephadex" G-2Q0 i 0,05 M phosphatpuffer med pH 6,2. Fraktionerne, hvis højeste enzymaktivitetsprocent blev bundet ved hjælp af antistoffer overfor HCG, blev anvendt i prøvesystemet.
b) Fremstilling af antistoffer mod HCG·.
Antistoffer mod HCG· blev dannet i kaniner, som beskrevet af Schuurs et. al. i Acta Endocr. (Ebh.) 59,, 120 (1968).
c) Fremstilling af immunoadsorbenten, anti-HCG-cellulose.
γ-Globulinfraktionen af anti-HCG—serummet beskrevet under b) blev fremstillet ved udfældning med 18$ (vægt/volumen) fast U^SO^. Præcipitatet blev vasket og derefter optaget i så meget 0,05 M borat-puffer med pH 8,6, at den endelige proteinkoncentration blev 10 mg/ml.
M-aminobenzyloxymethyleellulose (350 mg), der var fremstillet ved hjælp af G-urvich's metode» som beskrevet i Biokhimiya 26, 934 (1961), blev suspen-deret i 50 ml destilleret vand og diazoteret ved tilsætning af 10 ml 36$ saltsyre og dråbevis 10 ml NaN02-opløsning. Suspensionen blev centrifugeret og vasket, og bundfaldet blev atter suspenderet i 43 ml 0,05 M natriumborat med pH 8,6. Af den fremstillede γ-globulinopløsning blev 7 ml sat til denne suspension. Blandingen blev omrørt i 26 timer ved 4°C, centrifugeret og til slut vasket med 1 liter 0,02 M phosphatpuffer med pH 6,0.
d) Bestemmelse af HCG· i serum.
Der blev fremstillet en fortyndingsrække af HCG- (8-4-2-1-0,5-0,25-0 I.E./ml) med en fortyndingsvæske bestående af 1 del menneskeserum og 11 150170 2 dele 0,05 M phosphatøuffer med pH 6,2. Af hver af de således ibamstillede HCG-fortyndinger blev 0,5 ml rotationsbehandlet i 2 timer ved
Stuetemperatur sanmep med 0,5 - ml: af inriiawadsorberitsuspensionen (4 mg /ml), fremstillet ifølge c), og derefter centrifugeret. Præcipitatet blev 5 vasket to gange, hver gang med 2 ml 0,05 M phosphatbuffer med pH 6,2. Præcipitatet blev blandet med' 1,0 ml HCG-HEP-opløsning i en passende fortynding samt i 0,05 M phosphatpuffer med pH 6,2 og atter rota-'-· tionsbehandlet ved stuetemperatur i 2 timer.
10 Efter centrifugering blev enzymaktiviteten bestemt i den overliggende væske ved at sætte 0,5 ml deraf til 1,5 ml af en substratopløsning indeholdende 10 μΐ 30*fo H2O2 og 20 mg 5-aminosalicylsyre i 150 ml 0. 02 M phosphalpuffer med pH 6,0. Efter 30 minutter blev ekstinktionen målt ved 460 nm.
15 I det beskrevne prøvesystem forårsagede en HCG-koncentration på 0,25 1. E./ml en målelig forøgelse af enzymaktiviteten i den ovenliggende væske, medens en koncentration på 1 I.E./ml forårsagede den maksimale forøgelse. Ved denne prøve viste centrifugeringstrinnet sig at være 20 af afgørende betydning, da udeladelse af dette trin førte til forkerte måleresultater for enzymaktiviteten, bl.a. på grund af uklarhed i serummet og dett§s peroxidaselignende aktivitet.
HCG-indholdet i gravide kvinders serum kunne bestemmes ved 25 denne forsøgsopstilling, forudsat at serumprøven blev fortyndet i forholdet mindst 1:3.
Eksempel 2 3q Bestemmelse af HCG i lave koncentrationer ved hjælp af et enzym/an-tigenkoblingsprodukt.
a) Fremstilling af antistoffer overfor kanin-γ-globulin.
kanin-v-globulin blev isoleret fra normalt kaninserum ved at ud-35 fælde det med 18fo (vægt/volumen) fast NagSO^. Antistoffer mod det blev dannet i et får. Injektionsskemaet var: 12 150170 . Dag - Mængde Freund*s hjælpestof In.iektionsmåde O 0,5 mg + Intramuskulært 14 0,5 mg + ” 5 28 1 mg + " 42 1 mg - Intravenøst 56 1 mg - " 10 På dag nr. 70 blev fåret tappet for blod.
b) Fremstilling af /iåre-anti-(kanin-y-globulin)_7-cellulose.
Fåreserummets γ-globulinfraktion, som er beskrevet yqder a), blev fremstile 15 let ved udfældning deraf med 16% (vægt/volumen) fast natriumsulfat. Denne γ-globulinfraktion blev bundet til m-aminobenzyloxymethyl-cel= lulose, som beskrevet i eksempel 1 c).
c) Bestemmelse af humant chorion3.sk gonadotropin (HCG).
20
Der blev fremstillet en fortyndingsrække af HCG i 0,01 M phosphatpuffer med pH 6,0, som også indeholdt 2$ (volumen/volumen) normalt fåreserum. Fortyndingsrækken var i området 10 til 520 I.E./l, idet fortyndingsfaktoren var 2.
25
Til 5 ml af en HCG-opløsning blev der tilsat 0,1 ml af et fåre-(anti-HCG)—serum (se eksempel lb)), der var fortyndet med den samme puffer til den ønskede styrke. Men jilod blandingen henstå ved stuetemperatur i 30 minutter, hvorefter der blev tilsat 1,5 mg./iåre-anti(kanin-γ-30 globulin)7-cellulose, og blandingen blev rotationsbehandlet i 2 timer.
Cellulosen blev centrifugeret i 10 minutter ved 3000 o.p.m. og atter suspenderet i 1 ml af en opløsning af HCG-HRP-koblingsprodukt, fremstillet ifølge eksempel 1 a), fortyndet til den ønskede styrke med 35 0,01 M phosphatPuffer med pH 6,0 med 2$ normalt fåreserum. Blandingen blev atter omrørt i 2 timer. Efter centrifugering bLev enzymaktiviteten bestemt i den overliqgende væske ved at sætte 0,5 ml deraf til 1,5 ml enzymsubstrat bestående af 10 μ1 30$ HgOg og 20 mg 5-aminosalicylsyre i 150 ml 0,01 M phosphatpuffer med pH 6,0. Man lod blandingen henstå i 30 minutter ved 25°C, hvorefter ekstink- 150170 13 tionen "blev målt ved 460 run. I den overliggende væske måles 100$ enzymaktivitet, forudsat at intet anti-HCG-serum er sat til systemet.
5 En fortyndingsrække af HCG-, fremstillet med børneurin som fortyndingsvæske, viste et identisk mønster, således at også målinger i urinprøver kan udføres.
Centrifugeringstrinnet bevirker en ti gange større følsomhed end den der kan opnås i et system uden centrifugering.
Eksempel 3
Bestemmelse af HCG og EH i lave koncentrationer ved hjælp af et en- zym/antistofkoblingsprodukt.
15 a) Eremstilling af immunoadsorbent-HCG-cellulosen.
Denne immunoadsorbent blev fremstillet ved hjælp af den i eksempel le) omtalte metode, men i stedet for kanin-y-globulin blev 20 100 mg HCG koblet til 500 mg m-aminobenzyloxymethylcellulose.
b) Rensning af antistoffer mod HCG.
10 ml Kanin-anti-HCG-serum, fremstillet ifølge eksempel lb), blev 25 fortyndet med 90 ml 0,05 M citrat med pH 5,0 og iåncrsomt ledt over immunoadsorbenten, som var pakket i en søjle og blandet med 10 dele "Sephadex" G-25. Immunoadsorbenten blev vasket med den samme puffer, indtil der ikke længere blev elueret protein. Antistofferne blev elueret med 0,05 M citrat med pH 2,0. Eraktionerne blev opsamlet i 30 1/2 rumfang 0,25 M HaHCO^, afprøvet for deres indhold af antistoffer og protein, og de egnede fraktioner blev frosset.
c) Eremstilling af koblingsproduktet (anti-HCG)-HRP.
20 mg Peberrodperoxidase (HBP) 'blev opløst i 2 ml af en antistofop-35 løsning med et proteinindhold på 2 mg/ml. Til denne opløsning blev der tilsat 8 μΐ 25$ glutaraldehydopløsning, hvorefter blandingen blev rystet i 2 timer ved stuetemperatur. Til slut blev blandingen fraktioneret over en "sephadex" G-20Q søjle i o,05 M phosphatpuffer med pH
14 150170 6,5. Fraktionerne, livis højeste enzymaktivitetsprocent blev bundet til HCG-cellulosen, blev anvendt i prøvesystemet.
d) Bestemmelse af HCG og IH.
5 10 ml Af en HCG-fortyndingsrække af HCG og 10 ml af en HCG-fortyn-dingsrække af IH blev blandet med 5 mg anti-HCG-cellulose, fremstillet ifølge eksempel 1 c), som blev suspenderet i 1 ml 0,15 M phos-pha tpuf fer med pH 6,0, og blandingen blev rotationsbehiandlet ved stuetemperatur 10 12 timer. Immunoadsorbenten blev centrifugeret og vasket med 5 ml 0,05 M phosphatbuffer med pH 6,0.
Immunoadsorbenten blev tilsat 1 ml af (anti-HCG)-HRP-koblingspro-duktet i den ønskede fortynding,, hvorefter blandingen atter blev ro-12 tationsbehandlet i 2 timer. Til slut blev enzymaktiviteten i den overliggende væske bestemt efter centrifugering som beskrevet i de foregående eksempler.
Ted hjælp af denne metode kunne en koncentration på henholdsvis 5-10 2o I.E. HCG og 10-20 I.E. IH pr. liter bestemmes. Hvis centrifugeringstrinnet udelades, er den optimale prøvestørrelse 0,5 ml og følsomheden ea. 100 I.E. HCG pr. liter eller ca. 200 I.E. IH pr. liter, således at fremgangsmåden ifølge opfindelsen bevirker en 10-20 ganges forøgelse af følsomheden.
25
Eksempel 4
Bestemmelse af HCG og anti-HCG.
a) Kaninserum blev fraktioneret over ’ DEAE-cellulose i overensstemmelse med fore-30 skriften ifølge H.A. Sober og andre i J. Am. Chejru Sog. 78f 756 (19561. Den isolerede γ-globulinfraktion, som var immuno-elektroforetisk ren, blev dels anvendt til dannelse af antistoffer- i et får i overensstemmelse med skemaet i eksempel 2 a), medens desuden 100 mg kanin-γ-globulin blev koblet til 500 mg m-aminobenzyloxymethylcellulose ved 35 hjælp af metoden beskrevet i eksempel .1 c).
Udfra det fremstillede fåre-/anti-(kanin-Y-globulin)_7-serum blev de specifikke antistoffer isoleret ved metoden· beskrevet i eksempel 3 b) med den fremstillede immunoadsorbent,· 15 150170 b) Koblingsproduktet /anti-(kanin-γ-globulin)]-HEP blev fremstillet analogt med koblingsproduktet (anti-HCG·)-HEP beskrevet i eksempel 3 c) .
5 c) Bestemmelse af anti-HCG·.
En fortyndingsrække af kanin-(anti-HCG·)-serum blev fremstillet med 0,05 M phosphatpuffer med pH 6,0.
10 Kanin-(anti-HCG·)-serum (0,5 ml blev rotationsbehandlet sarrmen med 0,25 mg'HCG-cellulose i 2 timer (se eksempel 3a)). Reaktionsblandingen blev centrifugeret, og præcipitatet blev vasket fire gange med phosphatpuf fer,, hver gang med 3 ml , hvorefter præcipitatet blev resuspenderet i 1 ml af en opløsning af koblingsproduktet b . Ben opnåede blanding blev rotationsbehandlet i 2 timer. Efter centrifugering blev enzym-aktiviteten i den overliggende væske bestemt som beskrevet i eksempel 1 d).
d) Bestemmelse af HCG.
Med de fremstillede reagenser blev HCG bestemt ved at inkubere op- 20 løsninger deraf sammen med 0,5 ml kanins (anti-HCG)-serum i en fortynding, som i systemet beskrevet under c) netop forårsager en næsten maksimal reduktion af énzymaktivitet i.den overliggende væske, og ved at gennemføre fremgangsmåden beskrevet under c) med den opnåede blanding.
25 Når man brugte 5 ml HCG-opløsning, viste det sig at være muligt at bestemme koncentrationer på ca. 10 X.E./l HCG.
Eksempel 5 30. --
Bestemmelse af insulin i serum, a) Fremstilling af insulin-(glucose-oxidase).
5 mg svineinsulin og 25 ml glucose-oxidase blev opløst i 2 ml 0,05 35 M phosphatpuffer med pH 6,5. Til denne opløsning sattes 5 jul 25$ glutaraldehydopløsning, hvorefter blandingen blev rystet ved stuetemperatur i 90 minutter. Blandingen blev fraktioneret over "Sephadex" G-200 i0,05 M phosphatpuffer med pH 6,5· Fraktionerne, hvis højeste procent enzymaktivitet kunne bindes ved hjælp af 40 antistoffer mod insulin, blev anvendt i prøvesystemet.
16 150170 b) Fremstilling af antistoffer mod insulin.
10 marsvin blev 1 gang om ugen injiceret intramuskulært med 1 mg svi-neinsulin i Freund's komplette hjælpestof i et tidsrum på 4-8 uger. Efter at være ladt alene i 2 uger blev dyrene injiceret intravenøst 5 med yderligere 1 mg insulin uden hjælpestof. Yderligere 2 uger senere blev dyrene tappet for blod. Hypogly-kæmi, som forekommer lejlighedsvis, blev bekæmpet ved intraperitoneal administration af glucose.
c) Fremstilling af antistoffer mod marsyin-y-globulin.
10
Marsvin-γ-globulin blev fremstillet ved at sætte 1 rumfang af en mættet ammoniumsulfatopløsning til 2 rumfang marsvineserum. Eet resulterende præcipdiat blev vasket 2 gange med'33# mættet (NH^gSO^-opløs-ning og derefter optaget i en fysiologisk saltopløsning. Får blev 15 Immuniseret med stigende doser af det fremstillede γ-globulin, nemlig 0,5, 1 og 2 mg. Injektionerne blev givet hver anden uge, idet immunogene t blev blandet med Freund's komplette hjælpestof. 2 uger efter den sidste injektion blev der -indgivet yderligere 2 mg γ-globulin.
1 en fysiologisk saltopløsning. 1 Uge senere blev dyret tappet for 20 tlod- d) Eremstilling af uopløselige antistoffer mod marsvin-Y-globulin.
10 g Mikrokrystallinsk cellulose blev aktiveret ved under emrøring at blive sat til 400 ml 2,5% (vægt/volumen) CNBr-opløsning, hvorefter pH-vær-dien blev indstillet til 10,5 med en IN NaOH-opløsning, og den blev holdt på denne værdi i 2 minutter.' Cellulosen blev vasket med isvand og med 0,1 M NaHC03. Til 10 ml fåre-anti-(marsvin-y-globulinl-serum sattes 1,6 g-Na^O^. Efter omrøring i 1 time ved stuetemperatur blev præcipitatet centrifugeret fra, vasket 2 gange med 20 ml 16% (vægt/ volumen) Na2S04-opløsning og til slut optaget i 1Q ml 0,1 .M NaHCO^.
Een aktiverede cellulose blev blandet med 40 ml af en 0,1 M NaHCO,- 5 opløsning og 10 ml af γ-globulincipløsningen. Eenne suspension blev rotationsbehandlet i 40 timer ved 4°C og .vasket, 2 gange med 5 ml Q,5 M NaHCC , 2 gange med 500 ml 0,Q5 JA citrat med pH 1,1 og 2 gange med 5QQ ml 0,05 M phosphat med pH 6,2.
17 150170 e) Bestemmelse af insulin i serum.
4 ml Af en insulinfortyndingsrække i området fra 0 til 100 ng/ml blev ved stuetemperatur i 4 timer inkuberet sammen med 1,0 ml anti-insulin-5 serum (sattmen med 0,15 M phosphatpuffer med pH 6,0, for tandet til· den ønskede styrke). ’Derefter tilsattes 5 mg af den ifølge d) fremstillede -irtmunoadsor-bent, suspenderet i 1 ml 0,15 M phosphatpuffer med pH 6,0, og den resulterende blanding blev rotationsbehandlet, natten over ved 4°C. Im-munoadsorbenten hlev derpå centrifugeret og vasket 3 gange med 5 ml 0,05 M phosphatpuffer med pH 6,0 (hver gang med 5 ml), hvortil der var blevet tilsat 2$ fåreserum. Derefter blev 1,0 ml insulin-glucose-oxidase,fortyndet til den ønskede styrke med vaskepufferen, sat til immunoadsorbenten. Den opnåede blanding blev igen rotationsbehandlet natten over og centrifugeret,·· ·. hvorefter enzymaktiviteten i den overlig— 15 gende væske blev målt ved at inkubere 0,5 ml deraf sanmen med 2,5 ml af en substratopløsning, og ekstinktionen blev målt ved 460 nm. Substratopløsningen indeholdt 50 mg glucose, 10 yxg peroxidase og 1 mg 5-ami-nosalicylsyre pr. 2,5 ml 0,05 M phosphatpuffer med pH 6,0.
20 Centrifugeringstrinnet, som i dette tilfælde tjener til både at øge det maksimale volumen prøvevæske, som kan anvendes, og til at fjerne serumfaktorer, som forstyrrer reaktionen, forårsagede en 10 ganges forøgelse af følsomheden, således at en koncentration på få ng/ml insulin kunne påvises.
25
Eksempel 6
Bestemmelse af østradiol.
a) Eremstilling af østradiol-17-succinyl-HEP.
30 50 mg Østradiol-17-hæmisucoinat og 0,08 ml tri-n-butylamin blev opløst i 2,5 ml dioxan. Til den kolde opløsning (2°C) blev der tilsat 15 fiX isobutylchlorcarbonat. Efter 30 minutter blev denne opløsning blandet med 100 mg peberrodperoxidase (HEP) i 7,5 ml af en blanding 25 af dioxan og vand (2:3), som var blevet indstillet til pH 9,5 med kaustisk soda. Denne opløsning blev omrørt i 4 timer ved 2°C, hvorefter den blev dialyseret i 18 timer. Præcipitatét, som opnåedes efter at dialysatets pH-værdi var blevet indstillet til 4,6, blev centrifugeret fra, vasket og optaget i 5 ml destilleret vand, som var blevet 18 150170 indstillet til pH 8. Materialet blev yderligere renset Ted at udfælde det 2 gange med 10 ml acetone. Sintproduktet blev optaget i 10 ml 0,05 M phosphatpuffer med pH 7,8.
5 b) Fremstilling af østradiol-17-succinyl-BSA.
Præparatet bley fremstillet ved hjælp af den blandede anhydrid-metode som beskrevet under a), Udgangsmaterialet var 100 mg øs tradio 1-17-hæmisuecinat og 150 mg kvægse rumalbumin (BSA).
10 c) Fremstilling af antistoffer for østradiol.
Et får blev hver fjerde uge injiceret med 4 mg østradiol-17-succinyl-BSA i Freund's komplette hjælpestof. Med regelmæssige interval-··, ler blev der udtaget blod fra fåret. Serummet blev adsorberet med 15 BSA.
d) Fremstilling af antistoffer mod fåre-γ-globulin.
Fåre-V-globulin blev fremstillet som beskrevet i eksempel 2b), men 20 denne gang med 16$ (vægt/volumen) natriumsulfat. Kaniner blev immuniseret med de&te fåre-γ-globulin ifølge følgende skema:
Bag Mængde Freund's hjælpestof In.iektionsmåde 0 200 pt>g + Intramuskulært 25 14 400 ,ug + ” 28 800 μβ + " 42 800 μβ - Intravenøst 30 2 TJger efter den sidste injektion blev dyrene tappet for blod.
e) Fremstilling af immunoadsorbenten /kanin-anti(-fåre-γ-globulin)J-cellulose.
35 γ-Globulinfraktionen af antiseraene beskrevet under bl blev fremstillet ved udfældning med 18$ (vægt/volumen) Ha2S0^. Bet opnåede produkt blev koblet med cellulose ved hjælp af Gurvich's metode SOm beskrevet i eksempel 1 cl.
19 150170 f) Bestemmelse af østradiol.
En fortyndingsrække af østradiol (0-0,5-1-2-4-8-16 ng/ml) blev fremstillet i phospha tpuf fer med pH 6,0. 5 ml Prøve blev blandet med 5 0,5 ml fåre-anti-østradiol-serum i den ønskede fortynding. Efter inkubering af blandingen i 2 timer ved stuetemperatur tilsattes 1 ml immunoadsorbentsuspension {ée e) indeholdende 60 mg/ml, hvorefter blandingen blev rotationsbehandlet i 4 timer ved stuetemperatur. Cellulosen blev centrifugeret fra/ og vasket med 5 ml 0,05 M phosphatpuffer med pH ‘ 10 6,0 indeholdende 2$ BSA. Derefter blev 1 ml østradiol-17-succinyl- HEP, fortyndet til den ønskede styrke med pufferen, 'hvormed blandingen blev våsket, i sat til cellulosen. Blandingen blev rotationsbehandlet i 1 time, hvorefter den atter blev centrifugeret, og enzymaktiviteten i den ovenstående væske måltes, som beskrevet 15 i eksempel 1.
Yed hjælp af den beskrevne metode kunne' koncentrationer på 1 ng/ml østradiol bestemmes, hvilket betyder en forøgelse i følsomheden med en faktor på 10 sammenlignet med prøven uden centrifugerings-20 trin.
Eksempel 7
Bestemmelse af cortisol.
25 a) fremstilling af cortisol-21-galactose-oxidase.
50 mg Cortisol-21-hæmisuccinat og 100 mg galactose-oxidase blev koblet ved hjælp af den blandede anhydrid-metode, som beskrevet i eksempel 6 a).
30 b) fremstilling af uopløseligt transcortin.
100 mg Transcortin, der var renset ved hjælp af DEAE-ce'llulosekromatografi efterfulgt af hydroxylapatitkromatografi, blev koblet med 5 g £epha-rose 4B ved hjælp af CNBr-metoden: Sepharose 4B-suspension (5 g) blev aktiveret ved at blande den med 4 ml 2,5$ (vægt/volumen) CIBr-opløsning i destilleret vand, hvorefter pH blev indstillet med 1 U HaOH til mellem 10 og 11, ved hvilken værdi deh blev holdt i 6 mi-' nutter. Derefter blev sepharosen vasket med isvand og med 0,1 M
40
Claims (3)
150170 NaHCO^, hvorefter der blev tilsat 100 mg transcortin i 20 ml 0,1 M NaHCO^, og suspensionen Hev rystet ved 4°C i 24 timer. Efter at være blevet vasket i rækkefølge med 0,5 M IfaHCO^, 0,05 M citratpuffer med pH 1,1 og 0,05 M phosphatpuffer med pH 6,0 blev sepharosen 5 holdt i den sidste puffer, som blevet tilsat 0,1% merthiolat. c) Bestemmelse af cortisol. En cortisolfortyndingsrække i området fra 0,25 til 16 ng/ml blev 1° fremstillet i 0,05 M phosphatpuffer med pH 6,0) .';5 ml af hver corti-- solopløsning (i 0,05 M phosphatpuffer med jsH 6,0) blev rotationsbehandlet natten over med 5 mg trans c o r t in- isephar o s e ved 4°C. Efter centrifugering tiisattearl ml-coxtisol-21-galactose-oxidaseopløsning, fortyndet til en passende .koncentration i den tidligere nævnte puffer, hvorefter. 15 blandingen blev rotationsbehandlet i 2 timer ved 4°C.' Efter recentri-> fugering bestormes enzymaktiviteten i - den ovenstående væske ved at sætte 0,5 ml deraf til 1,5 ml substrat indeholdende 100 mg D-galactose, 20 mg 5-aminosalicylsyre og 10 jug peroxidase i 150 ml 0. 02 M phosphatpuffer med pH 6,0. Efter 30 minutter blev ekstink-20 tionen til slut målt ved 460 nm. Ved hjælp af denne metode kunne ca. 1 ng/ml cortisol bestemmes, hvilket betyder en forøgelse af følsomheden med en faktor på 10.
25 Patentkrav.
1. Fremgangsmåde til bestemmelse af et antigen eller dets tilsvarende antistof ved udnyttelse af sådanne 30 komponenters kendte bindingsaffinitet, kendetegnet ved, at komponenten, der skal bestemmes, omsættes med sin bindingspartner, som er insolubiliseret eller bliver insolu-biliseret, at den faste fase skilles fra den flydende fase, . at den faste fase derpå omsættes med en immunologisk kompo-35 nent, der er i stand til at reagere med en i den faste fase tilstedeværende komponent, hvorhos den immunologiske komponent er koblet til et enzym, og ,at den flydende eller faste fases enzymaktivitet til slut bestemmes, hvilken aktivitet er et mål for mængden af det stof, der skal bestemmes.
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USRE31006E (en) * | 1968-09-24 | 1982-08-03 | Akzona Incorporated | Process for the demonstration and determination of reaction components having specific binding affinity for each other |
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US4203802A (en) * | 1971-05-14 | 1980-05-20 | Syva Company | Inhibitable enzyme amplification assay |
US3875011A (en) * | 1972-11-06 | 1975-04-01 | Syva Co | Enzyme immunoassays with glucose-6-phosphate dehydrogenase |
US3904367A (en) * | 1973-08-15 | 1975-09-09 | Gen Electric | Contrast enhancement for immunological film detection |
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Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
SE341239B (da) * | 1967-09-06 | 1971-12-20 | Pharmacia Ab | |
US3654090A (en) * | 1968-09-24 | 1972-04-04 | Organon | Method for the determination of antigens and antibodies |
-
1971
- 1971-02-10 NL NL717101728A patent/NL154600B/xx not_active IP Right Cessation
-
1972
- 1972-01-27 US US00221447A patent/US3791932A/en not_active Expired - Lifetime
- 1972-01-27 ZA ZA720548A patent/ZA72548B/xx unknown
- 1972-02-01 GB GB469672A patent/GB1363565A/en not_active Expired
- 1972-02-02 AU AU38552/72A patent/AU468151B2/en not_active Expired
- 1972-02-04 CH CH165572A patent/CH573115A5/xx not_active IP Right Cessation
- 1972-02-07 CA CA134,026A patent/CA958314A/en not_active Expired
- 1972-02-08 FR FR7204056A patent/FR2126760A5/fr not_active Expired
- 1972-02-08 FI FI341/72A patent/FI53894C/fi active
- 1972-02-09 JP JP47014295A patent/JPS5247011B1/ja active Pending
- 1972-02-09 DK DK058072A patent/DK150170C/da not_active IP Right Cessation
- 1972-02-09 BR BR729/72A patent/BR7200729D0/pt unknown
- 1972-02-09 SE SE7201498A patent/SE451098B/xx unknown
- 1972-02-09 ES ES399608A patent/ES399608A1/es not_active Expired
- 1972-02-09 DE DE2206103A patent/DE2206103B2/de not_active Ceased
- 1972-02-10 BE BE779209A patent/BE779209A/nl not_active IP Right Cessation
-
1978
- 1978-05-11 CA CA303,100A patent/CA1040082B/en not_active Expired
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
USRE31006E (en) * | 1968-09-24 | 1982-08-03 | Akzona Incorporated | Process for the demonstration and determination of reaction components having specific binding affinity for each other |
Also Published As
Publication number | Publication date |
---|---|
FI53894B (fi) | 1978-05-02 |
US3791932A (en) | 1974-02-12 |
DK150170C (da) | 1987-06-29 |
CH573115A5 (da) | 1976-02-27 |
ZA72548B (en) | 1972-10-25 |
DE2206103B2 (de) | 1975-10-16 |
AU468151B2 (en) | 1973-08-09 |
CA958314A (en) | 1974-11-26 |
ES399608A1 (es) | 1974-11-16 |
NL7101728A (da) | 1972-08-14 |
FI53894C (fi) | 1978-08-10 |
NL154600B (nl) | 1977-09-15 |
GB1363565A (en) | 1974-08-14 |
SE451098B (sv) | 1987-08-31 |
BE779209A (nl) | 1972-05-30 |
FR2126760A5 (da) | 1972-10-06 |
CA1040082B (en) | 1978-10-10 |
BR7200729D0 (pt) | 1973-10-25 |
DE2206103A1 (de) | 1972-08-24 |
AU3855272A (en) | 1973-08-09 |
JPS5247011B1 (da) | 1977-11-29 |
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