DE2155658C3 - Verfahren zum Nachweis und zur Bestimmung von einem Hapten oder dessen Antikörper - Google Patents
Verfahren zum Nachweis und zur Bestimmung von einem Hapten oder dessen AntikörperInfo
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- DE2155658C3 DE2155658C3 DE2155658A DE2155658A DE2155658C3 DE 2155658 C3 DE2155658 C3 DE 2155658C3 DE 2155658 A DE2155658 A DE 2155658A DE 2155658 A DE2155658 A DE 2155658A DE 2155658 C3 DE2155658 C3 DE 2155658C3
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- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/964—Chemistry: molecular biology and microbiology including enzyme-ligand conjugate production, e.g. reducing rate of nonproductive linkage
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/975—Kit
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S436/00—Chemistry: analytical and immunological testing
- Y10S436/807—Apparatus included in process claim, e.g. physical support structures
- Y10S436/808—Automated or kit
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S436/00—Chemistry: analytical and immunological testing
- Y10S436/815—Test for named compound or class of compounds
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S436/00—Chemistry: analytical and immunological testing
- Y10S436/815—Test for named compound or class of compounds
- Y10S436/817—Steroids or hormones
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- General Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Peptides Or Proteins (AREA)
- Enzymes And Modification Thereof (AREA)
Description
'5
Zum Nachweis und zur Bestimmung niedermolekularer Substanzen, die in geringen Konzentrationen
vorliegen, wie Steroidhormonen in Körperflüssigkeiten, wurden Verfahren entwickelt, bei denen Proteine
verwendet werden, die fähig sind, die nachzuweisende 3<> Substanz spezifisch zu binden. Diese Verfahren beruhen
auf der Konkurrenz zwischen der nachzuweisenden Substanz in der Probe und einer bekannten Menge
der gleichen Substanz, die radioaktiv markiert ist, mit einer begrenzten Menge des spezifischen bindenden
Proteins. Durch die unbekannte Menge der bindungsfähigen Substanz wird bestimmt, welcher Anteil der
radioaktiv markierten Substanz an das spezifische bindende Protein gebunden wird.
Es ist auch möglich, mit Hilfe dieser Verfahren, eine unbekannte Menge eines spezifischen bindenden Proteins
durch Umsetzung einer Probe, die eine unbekannte Menge des spezifischen bindenden Proteins
enthält, mit einer bestimmten Menge einer bindungsfähigen radioaktiv markierten Substanz zu bestim- *5
men.
In der Literatur ist es üblich, diese Bestimmungsverfahren, je nach Art des verwendeten spezifischen
bindenden Proteins zu unterscheiden, obwohl das grundlegende Prinzip all dieser Bestimmungen das
gleiche ist. So wird z. B. von »konkurrierenden Protein-Bindungsversuchen« gesprochen, wenn Rezeptor-
oder Transportproteine verwendet werden, die im Körper vorkommen und von »radioimmunologischen
Bestimmungen«, wenn Antisubstanzen verwen- 5S
det werden.
Für beide Arten von Bestimmungen sind radioaktiv markierte Substanzen erforderlich. Das Arbeiten mit
diesen Substanzen erfordert das Vorhandensein präziser Meßvorrichtungen, gut ausgerüstete Laboratorien
und ein qualifiziertes Personal. Diese hohen Anforderungen machen eine allgemeine Anwendung dieser
Bestimmungsverfahren besonders in kleineren Laboratorien unmöglich.
Aus der USA.-Patentschrift 35 05 019 ist ein Ver- 6S
fahren zur Bestimmung von Vitamin B 12 in einer wäßrigen Probe bekannt, bei dem ein wasserunlösliches
Polymer, an das Intrinsicfaktor gebunden ist, mit der zu untersuchenden Probe und radioaktiv markiertem
B 12 zusammengebracht wird. In Bull. Soc. Chem. Biol., 50, 1968, Nr. 5/6, S. 1169 bis 1178 ist
angegeben, daß es möglich ist, ein Antigen mit einem Enzym zu markieren und dann mit dem entsprechenden
Antikörper auszufällen. In Science, Vol. 168, 1970, S. 1347 und 1348 ist ein immunologisches Verfahren
zur Bestimmung von Morphin bekannt, bei dem Morphin mit einem Protein gekuppelt und das Konjugat
mir einem radioaktiv markierten Antikörper ausgefällt und die Radioaktivität des Niederschlages
gemessen wird.
Es ist Aufgabe der Erfindung, ein Verfahren zum Nachweis und zur Bestimmung von einem Hapten
oder dessen Antikörper zu entwickeln, das einfach und bequem durchgeführt werden kann, kein Arbeiten mit
radioaktiven Substanzen erfordert und in kurzer Zeit zu zuverlässigen reproduzierbaren Ergebnissen führt.
Diese Aufgabe wird gelöst durch ein Verfahren zum Nachweis und zur Bestimmung von einem Hapten
oder dessen Antikörper unter Ausnutzung der für derartige Substanzen bekannten Bindungsaktivität, das
dadurch gekennzeichnet ist, daß die Bestimmung mit einer bestimmten Menge eines Kopplungsproduktes
aus dem Hapten und einem Enzym und einem in unlösliche Form gebrachten Bestandteil der Reaktion
Hapten-Antikörper durchgeführt wird und die Enzymaktivität in der flüssigen oder festen Phase bestimmt
wird.
Haptene sind nach der Definition von K. Landsteiner
proteinfreie Substanzen mit einem Molekulargewicht bis zu ungefähr 1500, die mit spezifischen
Antikörpern reagieren, jedoch nicht selbst zur Bildung von Antikörpern führen können. Um jedoch trotzdem
Antikörper zu Haptenen bilden zu können, müssen die Haptene, bevor sie dem Testtier injiziert werden,
an Polypeptide gekuppelt werden. Daraus resultieren besondere Schwierigkeiten beim Arbeiten mit Haptenen.
Da es bekannt ist, daß durch die Kupplung einer immunogenen Komponente, z. B. eines Antikörpers
an ein unlösliches Polymer die Reaktionsfähigkeit einer solchen Komponente gegenüber dem entsprechenden
Antigen vermindert wird, war zu befürchten, daß ein Antikörper der gegen das Kupplungsprodukt
eines Haptens mit einem Protein (z. B. Albumin) gebildet worden ist und der anschließend durch Binden
an ein unlösliches Polymer unlöslich gemacht worden ist, mit dem reinen Hapten nicht mehr reagieren würde.
Umso mehr mußte der Fachmann davon ausgehen, daß ein solcher unlöslich gemachter Antikörper mit
einem Hapten, das auch noch an ein Enzym gekuppelt ist, nicht mehr reagieren würde. Da ein Hapten eine
niedermolekulare Substanz und ein Enzym ein voluminöser Proteinkomplex ist, mußte angenommen
werden, daß sowohl eine zu starke sterische Hinderung als auch besondere Schwierigkeiten beim Nachweis
des Haptens eintreten wurden. Das ist überraschenderweise nicht der Fall, sondern es hat sich gezeigt, daß
durch Verwendung eines derartigen Hapten-Enzym-Komplexes ein sehr empfindliches genau reproduzierbares
und einfaches Testverfahren zur Bestimmung von einem Hapten oder dessen Antikörper möglich
wird.
Bei der Bestimmung eines Haptens konkurriert dieses Hapten und sein Kopplungsprodukt mit einem
Enzym um eine bestimmte Menge des unlöslichen spezifischen Antikörpers. Je mehr Hapten die Probe
enthält, um so geringer ist die Chance, für das
Kopplungsprodukt aus dem löslichen Enzym und dem Hapten sich mit dem unlöslichen spezifischen Antikörper
zu verbinden und um so mehr des Kopplungsproduktes bleibt in der flüssigen Phase zurück, in der
die Enzymaktivität auf einfache Weise gemessen werden kann.
Bei der Bestimmung eines spezifischen Antikörpers mit den gleichen Reagentien treten der zu bestimmende
lösliche Antikörper und der unlösliche Antikörper in Konkurrenz um eine bestimmte Menge des Kopplungs-Produktes
ays dem Hapten und dem Enzym. Wenn der Gehalt an Antikörper in der Probe höher ist, wird
der unlösliche Antikörper weniger von dem Enzym-Kopplungsprodukt binden und folglich bleibt mehr
Enzym in der flüssigen Phase zurück.
Ein spezifischer Antikörper mit zwei oder mehr bindenden Stellen kann ebenfalls nach dem erfindungsgemäßen
Verfahren nachgewiesen und bestimmt werden, d. h. mit dem Enzym-Kopplungsprodukt und
dem Hapten in unlöslicher Form. Die flüssige Phase ao des Reaktionsgemisches kann dann das Kopplungsprodukt an den Antikörper gebunden enthalten und
in der festen Phase kann der Komplex aus Enzym-Kopplungsprodukt und Antikörper und dem in Wasser
unlöslichen Hapten enthalten sein. Je mehr des »5 zu bestimmenden Proteins in der Probe enthalten
ist, um so mehr Enzymaktivität besitzt die flüssige Phase.
Mit Hilfe einer Bestimmungskurve für ein bestimmtes System, bei dem der zunehmende Gehalt an dem
zu bestimmenden Hapten oder Antikörper gegen die gefundene Enzymaktivität, vorzugsweise in der flüssigen
Phase, aufgetragen ist, kann die Menge des in der Probe enthaltenen Haptens oder Antikörpers für
den gefundenen Wert für die Enzymaktivität abgelesen werden.
Das wichtigste Reagens für dieses Bestimmungsverfahren ist das Kopplungsprodukt aus dem Hapten
und einem Enzy.n, im folgenden auch Enzym-Kopplungsprodukt genannt, das einerseits mit dem spezifisehen
Antikörper über das Hapten reagieren kann und andererseits Enzymaktivität besitzt. Dieses Reagens
wird nach einem für ähnliche Produkte beschriebenen Verfahren hergestellt. Das zweite Reagens, die unlösliche
Komponente in dem Reaktionssystem dient zur Erleichterung der Trennung der verschiedenen enzymhaltigen
Fraktionen des Reaktionsgemisches. Die Zugabe dieses Reagenses führt zur Bildung einer festen
Phase neben einer flüssigen Phase.
Die Enzymaktivität einer Fraktion des Reaktions- 5<>
gemisches kann bestimmt werden, indem diese Fraktion mit einem Substrat und anderen Substanzen zur
Durchführung einer Enzymreaktion inkubiert wird. Besonders geeignet ist dabei eine Reaktion, bei der
eine gefärbte Verbindung gebildet oder entfernt wird, deren Absorption auch leicht quantitativ gemessen
werden kann. Vorzugsweise wird als Enzym eine Oxidoreduktase verwendet.
Haptene, die nach dem neuen Verfahren nachgewiesen werden können sind z. B. Steroide, Vitamin
B12, Folinsäure, Thyroxin und Trijodothyronin, releasing
factors, Histamin, Serotonin und andere biogene Amine, Digoxin, Digitoxin, Prostaglandine, Adrenalin,
Nor-Adrenalin, pflanzliche Hormone, wie Auxin, Kinetin, GibereMinsäure und Antibiotika, wie Peni- e5
cillin.
Das Verfahren zum Nachweis spezifischer Antikörper für Haptene kann angewandt werden, z. B. zur
Bestimmung von Antikörpern gegen Penicillin oder zur Bestimmung des Intrinsik-Faktors.
Im Folgenden wird die Erfindung durch allgemeine
und spezielle Beispiele näher erläutert.
Die Herstellung von Kopp.'ungsprodukten von Enzymen und Haptenen kann auf verschiedene Weise
durchgeführt werden. Einige Haptene können schon Gruppen besitzen, die mit reaktionsfähigen Gruppen
an der Oberfläche des Enzyms vernetzt werden können, während andere erst derartige Gruppen durch chemische
Reaktion erhalten müssen. Es ist selbstverständlich, daß die ursprünglichen Bindungseigenschaften
des Haptens und die Aktivität des Enzyms während dieses Verfahrens nicht wesentlich geändert werden
können. Die Gruppen des Enzyms, die besonders geeignet sind für Kopplungsreaktionen sind Amino- und
Carboxylgruppen. Wenn das modifizierte oder nichtmodifizierte Hapten ebenfalls derartige Gruppen besitzt,
kann die Kopplung z. B. durch Reaktion, wie sie aus der Peptidsynthese bekannt sind, durchgeführt
werden. Darüberhinaus können solche Substanzen, wie Glutaraldehyd, Difiuordinitrodiphenylsulfon, Toluoldiisocyanat,
Di- und Trichlor-s-triazin für die Kopplungsreaktion verwendet werden.
Spezielle Beispiele für die Kopplung von Haptenen mit Proteinen sind z. B. in Methods in Immunology
and Immunochemistry, Bd. 1, beschrieben. Die dort beschriebenen Verfahren werden angewandt zur Herstellung
von Kopplungsprodukten zur Immunisierung, sie können jedoch auch zur Herstellung von Kopplungsprodukten
des Haptens mit einem Enzym angewandt werden, die für das erfindungsgemäße Verfahren
wichtig sind.
Die Wahl des Enzyms, das eine Komponente für das Kopplungsprodukt aus Hapten und Enzym ist,
hängt ab von Eigenschaften wie der spezifischen Aktivität (eine hohe Umwandlungsrate vergrößert die
Empfindlickheit des Testsystems) und der Einfachheit der Bestimmung des Enzyms. Die Bestimmung eines
Enzyms, das eine Umwandlung katalysiert, bei der gefärbte Produkte entstehen oder verschwinden, ist
einfach. Derartige colorimetrische Bestimmungen können auf einfache Weise automatisiert werden.
Erfindungsgemäß ist es auch möglich, Enzyme zu verwenden, die Umwandlungen katalysieren, bei denen
Komponenten auftreten oder verschwinden, die spektrophotometrisch oder fluorimetrisch bestimmt werden
können. Diese Bestimmungen können ebenfalls automatisiert werden.
Für die Herstellung der Kopplungsprodukte sind Enzyme wie Katalase, Peroxidase, /3-Glukuronidase,
/?-D-Glukosidase, /S-D-Galactosidase, Urease, GIukose-oxidase
und Galactose-oxidase geeignet, bevorzugt wird die Gruppe der Oxidoreduktasen.
Der unlösliche spezifische Antikörper oder das unlösliche Hapten, die bei der erfindungsgemäßen Bestimmung
verwendet werden, können auf bekannte Weise, z. B. durch Vernetzung mit Chlor-ameisensäure-äthylester,
durch kovalente Bindung mit unlöslichen Trägern wie Agarose, Vernetzung mit Dextran
oder Filterpapier oder durch physikalische Kopplung an unlösliche Träger, wie Kunststoffe, hergestellt
werden.
Die Form, in der die Reagentien verwendet wenden
können, ist vielfältig. Die Komponente des Reaktionssystems, die mit einem Enzym gekoppelt ist, kann
gefriergetrocknet oder in einem Puffer gelöst sein. Darüberhinaus kann ein fester Träger, z. B. ein Papier-
streifen, der mit dem Kopplungsprodukt imprägniert ist, verwendet werden.
Die unlösliche Komponente kann in Form von Teilchen verschiedener Form, wie Körner, Kugeln und
Stäbchen oder in Form eines Streifens des einen oder anderen Trägermaterial gebracht werden.
Zur Durchführung des erfindungsgemäßen Verfahrens kann eine Testpackung verwendet werden, die
hauptsächlich bestellt aus:
a) einer bestimmten Menge des Kopplungsproduktes aus einem Hapien und einem Enzym;
b) einer entsprechenden Menge einer der Komponenten des Reaktionssystems in unlöslicher Form;
c) einem Substrat zur Bestimmung der Aktivität des verwendeten Enzyms.
Wenn erforderlich, kann die Testpackung auch die notwendigen Hilfsmittel zur Herstellung einer Verdünnungsreihe
der zu untersuchenden Probe für eine quantitative Bestimmung, wie Reagenzgläser, Pipellen
und Kolben mit Verdünnungsmittel, enthalten.
Die Erfindung wird durch die folgenden speziellen Beispiele noch näher erläutert:
Bestimmung von Testosteron
A) Herstellung von Testosteron-3-HRP
A) Herstellung von Testosteron-3-HRP
100 mg Testosteron-3-(0-earboxymethyl)-oxim und
0,143 ml Tri-n-buiylamin wurden in 5ml Dioxan gelöst.
Die Lösung wurde auf 2 C abgekühlt und dann wurden 0.0" ml Isobutylchlorcarbonat zugegeben.
Nach 30 min wurde die Lösung zu 100 mg HRP (Meerrettichperoxidase) in einem Gemisch von 9 ml
Wasser und 6 ml Dioxan zugegeben und mit 0,1 η NaOH auf einem pH-Wert von 9 eingestellt. Diese
Lösung wurde 4 h bei 2 C gerührt und über Nacht dialysiert. Der Niederschlag, der nach Einstellung des
Dialysats auf einen pH-Wert von 4.6 erhalten worden war, wurde nachdem er über Nacht stehengelassen
worden war. zentrifugiert, in 10 ml Wasser suspendiert und mit Hilfe von Natronlauge gelöst. Das Material
wurde dreimal mit 15 ml Aceton bei einem pH-Wert von 4,5 ausgefällt, in 15 ml Wasser, das mit Natriumhydroxid-Lösung
auf einen pH-Wert von 7,8 eingestellt war, gelöst, dialysiert und schließlich lyophilisiert.
B) Herstellung von Testosteron-3-BSA
Dieses Kopplungsprodukt wurde auf die gleiche Weise wie das Testosteron-3-HRP hergestellt, wobei so
jedoch als Ausgangsmaterial 50 mg Testosteron-3-(O-carboxymethyl)-oxim
und 150 mg BSA (Rinderserumalbumin) verwendet wurden.
C) Herstellung von Antikörpern gegen Testosteron-3-BSA
5 Kaninchen wurden intramuskulär zunehmende Dosen von Testosteron-3-BSA in vollständigem
Freund'schen Adjuvans (0,5,1 und 2 mg) in Intervallen
von 3 Wochen injiziert. Zwei Wochen nach der letzten Injektion wurden den Tieren intravenös 2 mg Antigen
in physiologischer Kochsalzlösung injiziert. Eine Woche danach wurde den Tieren Blut abgenommen.
Die gegen BSA gebildeten Antikörper wurden entfernt, indem das Serum anteilweise mit BSA-m-amino- 6s
benzyloxymethylcellulose, die nach dem Verfahren
von Gurvich (siehe D) hergestellt worden war, behandelt wurde.
D) Herstellung von Antitestosteroncellulose
Diese Substanz wurde entsprechend dem von Gurvich in Biokhimiya 26,934(1961) beschriebenen Vcrfahren
hergestellt.
1. Herstellung von »Aminocellulose«:
50 g Whatman Cellulose, die mehrfach gewaschen und dekantiert worden war, wurden in 100 ml
ίο einer 0,7"„igen Natriumacetatlösung suspendiert,
die 2 g N(m-Nitrobenzoxy)-methylpyridin enthielt. Das Gemisch wurde bei 60 bis 80 C getrocknet
und 40 min auf 125 C erhitzt. Das entstehende Produkt wurde gründlich mit deslilliertem
Wasser gewaschen, bei 80 C getrocknet, mit Benzol gewaschen und erneut getrocknet. 50 g des
getrockneten Produktes wurden durch Suspension in 300 ml einer 15%igen Na2S2O4-Lösung reduziert
und 30 min bei 50 bis 60 C gerührt. Das
»o Produkt wurde filtriert und nacheinander mit destilliertem Wasser, 30%iger Essigsäure und
wieder mit destilliertem Wasser gewaschen.
2. Behandlung mit ammoniakalischer Kupferlösung:
>5 40 ml 10%iger Schwefelsäure, 20 ml 50%iger
Salpetersäure und 140 ml destilliertes Wasser wurden unter Rühren auf 90' C erhitzt. Anschließend
wurden 5,9 g CuO in kleinen Anteilen zugegeben. Die Lösung wurde 2 h zum Sieden erhitzt
)o und mit destilliertem Wasser auf 500 ml aufgefüllt.
80 ml dieser Lösung wurden in ein Eisbad gegeben und unter Rühren zu 160 ml kalter 4 η
NaOH zugegeben. Nach 30minütigem Rühren wurde der Niederschlag zweimal mit destilliertem
Wasser gewaschen und in 80 ml 25 %igem Ammoniak gelöst. Zu dieser Lösung wurde nach und
nach I g »Aminocellulose« zugegeben. Das Gemisch wurde 1V2 h gerührt und anschließend
wurden 40 ml siedendes Wasser zugegeben und die Lösung schnell auf 00C abgekühlt. Die Lösung
wurde mit 10%iger Schwefelsäure neutralisiert, worauf die Aminocellulose ausflockte. Sie wurde
mit kaltem destillierten Wasser gewaschen.
3. Herstellung von y-Globulin:
Zu Kaninchen Antitestosteronserum wurden 180 mg Na2SO4 pro ml Serum zugegeben. Das
Gemisch wurde 1 h bei Raumtemperatur gerührt und der entstehende Niederschlag zentrifugiert,
zweimal mit einer 18%igen Na2SO4-LoSUHg gewaschen und in so viel 0,05 m Natriumborat mit
einem pH-Wert von 8,6 aufgenommen, daß die Proteinkonzentration ungefähr 10 mg/ml betrug.
4. Bindung des /-Globulins an Aminocellulose:
350 mg »Aminocellulose« wurden in 50 ml destilliertem Wasser suspendiert. Die Suspension wurde
auf 00C abgekühlt. 10 ml 36%ige Salzsäure wurden zugegeben und anschließend 10 ml I0%ige
NaNO2-Lösung zugetropft. Die Suspension wurde
zentrifugiert, mit kaltem destillierten Wasser und anschließend mit 0,05 m Natriumborat mit einem
pH-Wert von 8,6 gewaschen. Die Cellulose wurde in 43 ml 0,05 m Natriumborat mit einem pH-Wert
von 8,6 suspendiert. Zu dieser Suspension wurden 7 ml der wie oben hergestellten y-JGlobulinlösung
zugegeben. Das Gemisch wurde 26 h bei 4° C gerührt, zentrifugiert und mit 0,02 m Phosphatpuffer
35
45
mit einem pH-Wert von 6,0 gewaschen. Von dem
Antiseruni jedes der 5 immunisierten Kaninchen wurde eine Cellulosesuspension hergestellt (A
bis E).
E) Bestimmung von Testosteron mit Hilfe von Testosieron-3-HRP
und Antiteslosteroncelliilose
Das folgende System wurde aufgebaut:
I) Immunrcaktioii
0,5 ml einer Probe, enthüllend Testosteron, 0,2 ml
Testosteron-.i-HRl1 {[00 mg/ml) und 0.3 ml einer
Aniitestosteroncellulose-Suspension wurden 2 h bei Raumtemperatur rotiert und dann 5 min mit
1000 g zentrifugiert.
Die Immunreaklion fand in 0,02 in Phosphatpuffer
bei einem pH-Wert von 6,0, enthaltend 2% Schafserum, statt.
II) Enzymrcaktion
0,5 ml der überstehenden Flüssigkeit wurden bei Raumtemperatur mit 1,5 ml Substrat 30 min
inkubiert. Die Extinktion wurde bei 460 nm gemessen.
Das Enzymsubstrat enthielt 10 μΐ, 30%iges
Wasserstoffperoxid und 20 mg 5-Aminosalicylsäure in 150 ml 0,02 m Phosphatpuffer mit einem
pH-Wert von 6,2.
Die Fig. I zeigt Meßwerte, bei denen Testosteron-3-HRP an die Antitestosteroncellulose-Zubereitungen
gebunden worden ist. In diesem Falle wurde nur Puffer als Probe in dem Testsystem
zugegeben. Wenn Cellulose an Stelle von Antitestosteroncellulose zugegeben wird, bleiben mehr
als 95% der Enzymaktivität in der überstehenden Flüssigkeit enthalten. Die Zubereitungen B, D
und E zeigten, daß fast kein Testosteron-3-HRP gebunden worden war, jedoch bei den Zubereitungen
A und C.
Fig. 2 zeigt die Ergebnisse der Inkubation einer Testosteronverdünnungsreihe mit Testosteron-3-HRP
bei vier verschiedenen Konzentrationen von Antistestosteroncellulose C.
mg/ml (I), 2 mg/m! (II), 4 mg/ml (III) und 16 mg/ml (IV). Es ist offensichtlich, daß mit diesem System eine
Menge von ungefähr 10 ng Testosteron gezeigt werden kann.
Beispiel 2
Bestimmung von Östradiol
Bestimmung von Östradiol
A) Östradiol-n-succinyl-HRP wurde hergestellt
durch die in Beispiel 1 A) beschriebene gemischte Anhydrid-Methode, wobei 50 mg Östradiol-17-hemisuccinat und 50 mg HRP als Ausgangsmaterialien verwendet wurden.
B) Östradiol-H-succinyl-BSA wurde nach der in
Beispiel 1 A) beschriebenen gemischten Anhydrid-Methode hergestellt, wobei 100 mg Östradiol-17-hemisuccinat und 150 mg BSA als Ausgangsmaterialien verwendet wurden.
C) Zur Herstellung der Antikörper geten östradiol-17-succinyl-BSA wurden 5 Kaninchen nach dem
in Beispiel 1 C) beschriebenen Schema immunisiert. Die Sera wurden mit BSA-m-Ammobenzyloxymethylcellulose absorbiert.
D) Antiöstradiolcellulose wurde auf die in Beispiel 1
D) für Anlitestosteroneellulose beschriebene Weise hergestellt. Von jedem der immunisierten Kaninchen
wurde eine Cellulosezubereitung hergestellt, die mit 16 bis einschließlich 20 numeriert wurden.
IZ) Die Untersuchung wurde analog derjenigen für Testosteron in Beispiel 1 L·) durchgeführt.
Die Fig. 3 und 4 zeigen einige Ergebnisse. Die ίο Fig. 3 zeigt, daß drei verwendbare Antisera durch die
Immunisierung erhalten wurden, on denen 17 den höchsten Titel besitzt. Die l-'ig. 4 zeigt das Testsystem,
bei dem Antiöstradiolcellulose 17 in einer Konzentration von 8 mg/ml verwendet wurde. Das System unterscheidet
nicht zwischen östron und 17 /3-Östradiol.
17 ,/-Östradiol, besonders Östriol, zeigen eine geringere
Kreuzreaktion. Testosteron und Progesteron beeinflussen das System nur in sehr hohen Konzentrationen.
Bestimmung von Antikörpern gegen Penicillin
Penicilloyl-Katalase
Penicilloyl-Katalase
30 mg Benzylpenicillinsäure wurden in 5ml96%igem Äthanol gelöst und zu 200 mg Katalase in 45 ml 0,1 m
Phosphatpuffer mit einem pH-Wert von 7,5 zugetropft. Die Reaktion wurde 2 h fortgesetzt, wobei der
pH-Wert mit 0,5 η NaOH zwischen 7,2 und 8,2 gehalten wurde. Das Reaktionsgemisch wurde gegen 6-31
0,02 m Phosphatpuffer mit einem pH-Wert von 7,0 dialysiert.
Auf die gleiche Weise wurden 250 mg Benzylpenicillinsäure an 5 g m-Aminobenzyloxymethylcellulose,
die nach dem Verfahren von Gurvich (Biokhitniya 26, 934 ['%!]) hergestellt worden war, gekoppelt.
Das Kopplungsprodukt wurde jedoch nicht dialysiert. sondern auf einem Glasfilter gewaschen.
Eine Überempfindlichkeit von Menschen gegenüber Penicillin konnte auf folgende Weise gezeigt werden:
0,2 ml einer Probe von nicht-hämolysiertem Serum wurden mit 0,5 ml einer Lösung von Penicilloyl-Katalase
(1:800) vermischt. Nach 30 min wurden 10 mg Penicilloyl-m-aminobenzyloxymethylcellulose
zugegeben. Das Gemisch wurde 30 min rotiert und anschließend die Enzymaktivität in der überstehenden
Flüssigkeit bestimmt, indem 0,02 ml dieser Flüssigkeit
zu 2,8 ml 0,05 m Phosphatpuffer mit einem pH-Wert von 6,8 zugegeben wurden, der 1,2 μΐ 30%iges H2O2
enthielt und anschließend die Abnahme der Extinktion bei 240 nm gemessen wurde. Im Serum von Patienten,
die gegenüber Penicillin überempfindlich waren, wurde eine geringere Enzymaktivität in der Flüssigkeit gefunden als bei Kaninchenserum. Die Werte für Menschen, die nicht überempfindlich waren, wichen nicht
wesentlich von denjenigen mit Kaninchenserum ab.
Bestimmung von Folinsäure
A) Herstellung von Folatglukoseoxidase
200 mg Glukoseoxidase (140 IU/mg) wurden in
10 mg PBS (mit Phosphat gepufferte Salzlösung,
eine phosphathaltige physiologische Kochsalzlösung) mit einem pH-Wert von 7,0 gelöst. 30 mg
1 -Cyclohexyl -3- (2-morpholinoäthyl) - carbodiimi d
(MCDI) wurden zugegeben und anschließend 24 mg Folinsäure. Die Reaktion dauerte 2 h und
anschließend wurde eine sorgfältige Dialyse gegen PBS mit einem pH-Wert von 7,0 durchgeführt.
B) Herstellung von Folat-MBSA (methyliertes Rin derserumalbumin) Folat-MBSA wurde hergestellt
nach dem von Ricker und StoI lar beschriebenen
Verfahren (Biochemistry 6, 2001 [1967]). 25 mg MCDI wurden zu 50 mg BSA in 50 ml
Wasser zugegeben und anschließend 20 mg Folinsäure. 2 h später hatte sich ein gelber Niederschlag
gebildet. Schließlich wurde das ganze Reaktionsgemisch eine beträchtliche Zeit gegen
physiologische Kochsalzlösung dialysiert.
C) Herstellung von Antiserum gegen Folat-MBSA
Am Tage 0, 21 und 42 wurden jeweils 4 Kaninchen intramuskulär 2 mg Folat-MBSA in vollständigem
Freund'schen Adjuvans und am Tage 35 intravenös 2 mg Folat-MBSA in physiologischer
Kochsalzlösung injiziert. Am Tage 49 wurde den Tieren Blut abgenommen.
D) Antifolatcellulose wurde entsprechend dem in Beispiel 1 D) beschriebenen Verfahren hergestellt.
E) Bestimmung von Folinsäure
100 μΙ der zu untersuchenden Probe und 700 μΙ
einer Antifolatcellulose-Suspension wurden 3 h rotiert. 200 μΐ Folatglukoseoxidase (1: !500) wurden
zugegeben. Das Gemisch wurde nochmals 3 h rotiert und zentrifugiert und anschließend die
Enzymaktivität in der überstehenden Flüssigkeit bestimmt. Diese Bestimmung wurde durchgeführt
durch Vermischen von 0,5 ml der überstehenden Flüssigkeit mit einer Lösung von 50 mg Glukose,
10 μg HRP und 1 mg 5-Aminosalicylsäure in
2,5 ml 0,05 η Phosphatpuffer mit einem pH-Wert von 6,0 und Messung der Extinktion nach 30 min
bei 460 nm.
Fig. 5 zeigt den Prozentsatz des gebundenen Enzyms gegen die Konzentration der Antifolatcellulose.
Fig. 6 zeigt die Empfindlichkeit des Testsystems in einer Antifolatcellulose-Konzentration von 2 mg/ml
und die Wirkung von Glycin, Asparagin, Alanin und Glutaminsäure.
Beispiel 5
Bestimmung von Digoxin
Bestimmung von Digoxin
A) Herstellung von Digoxin-HRP
Zu 22 mg Digoxin, in 1 ml abs. Äthanol suspendiert, wurde unter Rühren I ml 0,1 m
Natriummetaperjodat zugetropft. Nach 25 min wurden 0,3 ml 0,1 m Äthylenglykol zugegeben.
5 min spätur wurde dieses Gemisch unter Rühren zu einer Lösung von 32 mg Meerrettichperoxidase
(HRP) in I ml destilliertem Wasser zugetropft, das mit 5%iger K2CO3-Lösung auf einen pH-Wert von 9,5 eingestellt war. Während der Reaktion wurde der pH-Wert durch Zugabe 5%iger
K2CO3-Lösung auf 9 bis 9,5 gehalten. Als der pH-Wert stabil war, wurden 15 mg NaBH1 in 1 ml
destilliertem Wasser zugegeben. Nach 3 h wurde der pH-Wert mit 1 m Ameisensäure auf 6,5 eingestellt. 1 h später wurde 1 m NH4OH zugegeben,
bis ein pH-Wert von 8,5 erreicht war. Das Gemisch wurde über Nacht gegen kaltes fließendes
Wasser dialysiert. Schließlich wurde der pH-Wert mit 0,1 η Salzsäure auf 4,5 eingestellt. Das Gemisch wurde I h bei Raumtemperatur und 4 h
bei 4°C stehengelassen, um einen Niederschlag zu erhalten, der 1 h bei 1000 g zentrifugiert wurde.
Der Niederschlag wurde in 5 ml 0,1 m NaHCO3
gelöst, gründlich dialysiert und gefriergetrocknet.
B) Herstellung von Digoxin-BSA
Dioxiii-Rinderserumalbiimin (BSA) wurde auf
die gleiche Weise, wie sie oben für Digoxin-HRP angegeben ist, hergestellt, wobei jedoch von
436 mg Digoxin und 560 mg BSA ausgegangen wurde und die Mengen der anderen Reagenzen
in gleichem Verhältnis erhöht wurden wie das Dioxin.
C) Herstellung von Antikörpern gegen Dioxin
5 Kaninchen wurden 400, 800 bzw. 1600 μg
Dioxin-BSA im Abstand von 14 Tagen injiziert.
Das Immunogen wurde mit vollständigem Freund'-schen Adjuvans vermischt und intramuskulär verabreicht.
14 Tage nach der letzten Injektion wurde den Tieren intravenös 800 μg Digoxin-BSA in
physiologischer Kochsalzlösung injiziert. 10 Tage später wurde den Tieren das Blut entnommen.
Das Serum wurde mit BSA-m-Aminbenzyloxymethylcellulose
adsorbiert.
a5 D) Herstellung von Antidigoxincellulose
Antidigoxincellulose wurde nach dem Gurvich-Verfahren, wie unter 1 D) beschrieben, hergestellt.
E) Bestimmung von Digoxin
Eine Verdünnungsreihe wurde mit Digoxin in 0,1 m Phosphatpuffer mit einem pH-Wert von 7,5
hergestellt, enthaltend 0,9% NaCi, 0,5% Tween-20 und 1,0% BSA. Die Verdünnungsreihe ging von
0,1 bis 100 ng/ml. 1 ml einer Digoxin-Lösung wurde mit 0,1 ml Digoxin-HRP in einer geeigneten
Verdünnung vermischt und anschließend wurden 2 mg Antidigoxincellulose, die in 0,4 ml Puffer
suspendiert war, zugegeben. Das Gemisch wurde 6 h bei Raumtemperatur rotiert und anschließend
zentrifugiert und die Enzymaktivität in der überstehenden Flüssigkeit bestimmt.
Zugabe von 0,8 ng Digoxin führte zu einer meßbaren Zunahme der Enzymaktivität in der
überstehenden Flüssigkeit. Digoxin allein zeigte eine geringe Kreuzreaktion in dem System während
Cholesterin, Cortisol, Östradiol, Testosteron und Progesteron keine Kreuzreaktion in dem
System zeigten.
Beispiel 6
Bestimmung von Cortisol
Bestimmung von Cortisol
A) Herstellung von CortisoI-21-gaIactose-oxidase
50 mg Cortisol-21-hemisuccinat und 100 mg
Galactoseoxidase wurden nach dem in Beispiel 1 A) beschriebenen gemischten Anhydridverfahren
hergestellt.
100 mg Transcortin, das durch Chromatographie mit DEAE, Cellulose bzw. Hydroxylapatit
gereinigt worden war, wurden folgendermaßen mit Hilfe des CNBr-Verfahrens an 3 g Sepharose
4 B gekoppelt: 3 g Sepharose 4 B-Suspension wurden aktiviert durch Vermischen mit 4 ml einer
2,5%igen (Gewicht/Volumen) CNBr-Lösung in destilliertem Wasser und anschließend wurde der
pH-Wert mit 1 η NaOH auf 10 bis 11 eingestellt
und 6 min auf diesem Wert gehalten. Die Sepharose wurde mit Eiswasser und 0,1 m NaHCO3
gewaschen. Dann wurden 100 mg Transcortin in 20 ml 0,1 m NaHCO3 zugegeben und die Suspension
24 h bei 4 C geschüttelt. Dann wurde nacheinander mit 0,5 m NaHCO3, 0,05 m Citratpuffer
mit einem pH-Wert von 1,1 und 0,05 m Phosphatpuffer mit einem pH-Wert von 6 gewaschen und
die Sepharose in dem letzten Puffer gelassen, zu dem 0,1 % Merthiolat zugegeben worden war.
C) Bestimmung von Cortisol
0,5 ml einer cortisolhaltigen Probe (Standard, Plasma oder Urin) wurden zweimal mit Methylenchlorid
extrahiert (2 · 3 ml). Die vereinigten Auszüge wurde zur Trockne eingedampft. Der Rückstand
wurde in 0,5 ml physiologischer Kochsalzlösung aufgenommen und mit 0,2 ml Cortisol-21-galactose-oxidase
in einer geeigneten Konzentration und 0,3 ml Transcortin-Sepharose-Suspension ao
(5 mg/ml) vermischt. Das Gemisch wurde 15 min bei 4 C rotiert und zentrifugiert. Anschließend
wurde die Enzymaktivität in der überstehenden Flüssigkeit durch Zugabe von 0,5 ml dieser Flüssigkeit
zu 1,5 ml eines Substrats bestimmt. Das »5 Substrat bestand aus 100 mg D-Galactose, 20 mg
5-Aminosalicylsäure und 10 ,ug Peroxidase in
450 ml 0,02 m Phosphatpuffer mit einem pH-Wert von 6,0. 30 min später wurde die Extinktion
bei 460 mn gemessen.
5 ng/ml Cortisol in der Probe führten zu einer meßbaren Zunahme der Enzymaktivilät in der
überstehenden Flüssigkeit. Corticosteron und Progesteron beeinflussen d"s System nur, wenn größere
Mengen zugegeben wurde. Testosteron und Aldosteron besaßen kaum einen Einfluß.
Beispiel 7
Bestimmung von Transcortin
Bestimmung von Transcortin
Die zur Bestimmung von Cortisol, wie in Beispiel 6 beschrieben, verwendeten Reagentien wurden ebenso
zur Bestimmung von Transcortin verwendet.
Von einer Verdünnungsreihe von Transcortin von 0 bis 1280 ng/ml wurden 0,5 ml 15 min bei 4"C mit
0,2 ml Cortisol-21-galactose-oxidase in einer entsprechenden
Verdünnung inkubiert. Zu dieser Verdünnungsreihe wurden 0,3 ml Transcortin-Sepharose
(15 mg/ml) zugegeben und das Gemisch 15 min bei 4 C rotiert. Die Aktivität der überstehenden Flüssigkeit
wurde, wie in Beispiel 6 beschrieben, gemessen.
Eine Probe, enthaltend 40 ng/ml Transcortin, zeigte eine meßbare Zunahme der Enzymaktivität in der
überstehenden Flüssigkeit, während sich bei Gegenwart von 320 ng/ml die gesamte Enzymaktivität in der
überstehenden Flüssigkeit fand.
Hierzu 3 Blatt Zeichnungen
Claims (3)
1. Verfahren zum Nachweis und zur Bestimmung von einem Hapten oder dessen Antikörper unter
Ausnutzung der für derartige Substanzen bekannten Bindungsaktivität, dadurch gekennzeichnet,
daß die Bestimmung mit einer bestimmten Menge eines Kopplungsproduktes aus dem Hapten und einem Enzym und einem in unlösliche
Form gebrachten Bestandteil der Reaktion Hapten-Antikörper durchgeführt wird und die
Enzym-Aktivität in der flüssigen oder festen Phase bestimmt wird.
2. Verfahren nach Anspruch 1, dadurch gekennzeichnet, daß ein Vitamin oder Hormon als Hapten
verwendet wird.
3. Verfahren nach Anspruch 1 oder 2, dadurch gekennzeichnet, daß eineOxidoreduktase als Enzym
verwendet wird. *>
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
NL707016396A NL154598B (nl) | 1970-11-10 | 1970-11-10 | Werkwijze voor het aantonen en bepalen van laagmoleculire verbindingen en van eiwitten die deze verbindingen specifiek kunnen binden, alsmede testverpakking. |
Publications (3)
Publication Number | Publication Date |
---|---|
DE2155658A1 DE2155658A1 (de) | 1972-05-18 |
DE2155658B2 DE2155658B2 (de) | 1976-08-05 |
DE2155658C3 true DE2155658C3 (de) | 1978-09-14 |
Family
ID=19811504
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
DE2155658A Expired DE2155658C3 (de) | 1970-11-10 | 1971-11-09 | Verfahren zum Nachweis und zur Bestimmung von einem Hapten oder dessen Antikörper |
Country Status (16)
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US (1) | US3850752A (de) |
AU (1) | AU468060B2 (de) |
BE (1) | BE775187A (de) |
BR (1) | BR7107459D0 (de) |
CA (1) | CA967464A (de) |
CH (1) | CH617774A5 (de) |
DE (1) | DE2155658C3 (de) |
DK (1) | DK140268B (de) |
ES (1) | ES396741A1 (de) |
FI (1) | FI54033C (de) |
FR (1) | FR2113733A5 (de) |
GB (1) | GB1348935A (de) |
IT (1) | IT986829B (de) |
NL (1) | NL154598B (de) |
SE (1) | SE451162B (de) |
ZA (1) | ZA717192B (de) |
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Family Cites Families (2)
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US3615222A (en) * | 1968-09-04 | 1971-10-26 | New England Nuclear Corp | Method and apparatus for measuring the amount of a component in a biological fluid |
US3654090A (en) * | 1968-09-24 | 1972-04-04 | Organon | Method for the determination of antigens and antibodies |
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1971
- 1971-10-27 ZA ZA717192A patent/ZA717192B/xx unknown
- 1971-10-28 AU AU35082/71A patent/AU468060B2/en not_active Expired
- 1971-10-29 US US00193702A patent/US3850752A/en not_active Expired - Lifetime
- 1971-11-04 FI FI3155/71A patent/FI54033C/fi active
- 1971-11-06 ES ES396741A patent/ES396741A1/es not_active Expired
- 1971-11-08 CH CH1621671A patent/CH617774A5/de not_active IP Right Cessation
- 1971-11-08 DK DK546271AA patent/DK140268B/da not_active IP Right Cessation
- 1971-11-09 BR BR7459/71A patent/BR7107459D0/pt unknown
- 1971-11-09 GB GB5196171A patent/GB1348935A/en not_active Expired
- 1971-11-09 SE SE7114278A patent/SE451162B/xx unknown
- 1971-11-09 IT IT53970/71A patent/IT986829B/it active
- 1971-11-09 CA CA127,217A patent/CA967464A/en not_active Expired
- 1971-11-09 DE DE2155658A patent/DE2155658C3/de not_active Expired
- 1971-11-10 FR FR7140259A patent/FR2113733A5/fr not_active Expired
- 1971-11-10 BE BE775187A patent/BE775187A/nl not_active IP Right Cessation
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE2743445C2 (de) | 1976-09-29 | 1982-07-08 | Mochida Seiyaku K.K., Tokyo | Immunchemisches Haptenmeßverfahren durch Agglutinationshemmung |
Also Published As
Publication number | Publication date |
---|---|
FI54033B (fi) | 1978-05-31 |
FR2113733A5 (de) | 1972-06-23 |
BE775187A (nl) | 1972-03-01 |
IT986829B (it) | 1975-01-30 |
ES396741A1 (es) | 1975-05-16 |
DE2155658A1 (de) | 1972-05-18 |
GB1348935A (en) | 1974-03-27 |
DE2155658B2 (de) | 1976-08-05 |
AU468060B2 (en) | 1975-12-18 |
SE451162B (sv) | 1987-09-07 |
CH617774A5 (de) | 1980-06-13 |
AU3508271A (en) | 1973-05-03 |
FI54033C (fi) | 1978-09-11 |
BR7107459D0 (pt) | 1973-06-21 |
ZA717192B (en) | 1972-08-30 |
NL154598B (nl) | 1977-09-15 |
US3850752A (en) | 1974-11-26 |
CA967464A (en) | 1975-05-13 |
DK140268B (da) | 1979-07-16 |
NL7016396A (de) | 1972-05-15 |
DK140268C (de) | 1979-12-10 |
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