DE2651388A1 - Verfahren zur ermittlung einer antigen-antikoerper-reaktion oder protein/protein-reaktion - Google Patents
Verfahren zur ermittlung einer antigen-antikoerper-reaktion oder protein/protein-reaktionInfo
- Publication number
- DE2651388A1 DE2651388A1 DE19762651388 DE2651388A DE2651388A1 DE 2651388 A1 DE2651388 A1 DE 2651388A1 DE 19762651388 DE19762651388 DE 19762651388 DE 2651388 A DE2651388 A DE 2651388A DE 2651388 A1 DE2651388 A1 DE 2651388A1
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- 102000004169 proteins and genes Human genes 0.000 title claims description 51
- 108090000623 proteins and genes Proteins 0.000 title claims description 51
- 238000000034 method Methods 0.000 title claims description 20
- 238000006243 chemical reaction Methods 0.000 title claims description 7
- 239000002245 particle Substances 0.000 claims description 50
- 239000000427 antigen Substances 0.000 claims description 21
- 102000036639 antigens Human genes 0.000 claims description 21
- 108091007433 antigens Proteins 0.000 claims description 21
- 230000033001 locomotion Effects 0.000 claims description 7
- 239000000725 suspension Substances 0.000 claims description 7
- 239000007787 solid Substances 0.000 claims description 2
- 230000037230 mobility Effects 0.000 claims 5
- 238000013019 agitation Methods 0.000 claims 1
- 238000000149 argon plasma sintering Methods 0.000 claims 1
- 239000000243 solution Substances 0.000 description 16
- 239000000758 substrate Substances 0.000 description 7
- 239000004793 Polystyrene Substances 0.000 description 6
- 229920002223 polystyrene Polymers 0.000 description 6
- 238000005755 formation reaction Methods 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 210000002700 urine Anatomy 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 4
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- 238000005259 measurement Methods 0.000 description 4
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- 230000004520 agglutination Effects 0.000 description 3
- 230000009918 complex formation Effects 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 230000008105 immune reaction Effects 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000009597 pregnancy test Methods 0.000 description 2
- 239000012460 protein solution Substances 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 101710098119 Chaperonin GroEL 2 Proteins 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 238000005842 biochemical reaction Methods 0.000 description 1
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- 239000004033 plastic Substances 0.000 description 1
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Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N27/00—Investigating or analysing materials by the use of electric, electrochemical, or magnetic means
- G01N27/26—Investigating or analysing materials by the use of electric, electrochemical, or magnetic means by investigating electrochemical variables; by using electrolysis or electrophoresis
- G01N27/416—Systems
- G01N27/447—Systems using electrophoresis
-
- 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
- Y10S436/805—Optical property
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Molecular Biology (AREA)
- Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Electrochemistry (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Immunology (AREA)
- Pathology (AREA)
- Investigating Or Analysing Materials By Optical Means (AREA)
Description
1 River Road
Schenectady, N.Y./U.S.A.
Schenectady, N.Y./U.S.A.
Verfahren zur Ermittlung einer Antigen-Antikörper-Reaktion oder Protein/Protein-Reaktion
Die Erfindung betrifft die Ermittlung von Proteinen und insbesondere
ein Verfahren zur raschen Ermittlung spezifischer Antikörper in Lösungen.
In der DT-OS 24 33 246 werden ein verbessertes Verfahren und eine verbesserte Vorrichtung zur Ermittlung und Reinigung von
Proteinen und Antikörpern beschrieben. Nach dieser DT-OS sind immunologische Reaktionen hoch spezifische biochemische Reaktionen,
bei denen sich ein erstes Protein, das als Antigen bezeichnet wird, mit einem zweiten für das Antigen spezifischen
Protein vereinigt, das als Antikörper bezeichnet wird, wobei ein immunologisch komplexes Protein gebildet wird. Immunologische
Reaktionen in Organismen, z. B. von Tieren, sind für die Tiere bei der Bekämpfung von Krankheiten wesentlich. Nach einem
Verfahren, das nicht ganz bekannt ist, bewirkt das Eindringen eines fremden Proteins, d. h. des Antigens, daß der Organismus
ein Antikörper-Protein produziert, das spezifisch für das Antigen
ist. Die Antikörper-Proteinmoleküle besitzen reaktionsfähige
chemische ßindungsstellen, die denen des Antigenmoleküls ent-
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sprechen, so daß sich Antigen und Antikörper chemisch unter
Bildung eines immunologisch komplexen Proteins vereinigen.
In dieser DT-OS wird ausgeführt, daß das Sammeln und Reinigen von immunologisch aktiven Proteinen in der Vergangenheit
von den Fällungs- oder Agglutiniereigenschaften der Proteine
abhing, die von der immunologischen Komplexbildungsreaktion resultierten. Ein Beispiel für eine derartige Reaktion ist
der HCG-Proteinschwangerschaftstest. Dieser Test wird so durchgeführt, daß man eine bestimmte Menge eines HCG-Antiserums
in eine Urinprobe mischt. Es wird eine Anzahl von Polystyrolkugeln, die mit HGG-Protein überzogen worden sind,
danach in die zuvor hergestellte Urinprobe eingeführt. Die Polystyrolkugeln agglutinieren nur dann, wenn HCG-Protein
in der Urinprobe fehlt, da das HCG-Protein auf den Polystyrolkugeln
mit dem HCG-Antiserum einen Komplex bildet, das zuvor in die Probe eingeführt wurde. Wenn jedoch HCG-Protein in der
Urinprobe vorliegt, bildet das Protein mit dem zuvor eingeführten HCG-Antiserum einen Komplex, so daß sich ein Niederschlag
bildet, so daß kein Antiserum für eine Komplexbildung mit dem HCG-Protein auf den Kugeln zur Verfügung steht,
um ein Agglutinieren der Kugeln zu bewirken.
In dieser DT-OS wird festgestellt, daß man den HCG-Pro-
teinschwangerschaftstest dadurch vereinfachen kann, daß man
HCG-Antiserum auf Polystyrolkugeln aufträgt und unmittelbar eine Urinprobe testet. In einem derartigen Fall werden die
Kugeln nur dann agglutinieren, wenn HCG-Protein in der Probe
vorliegt. In dieser DT-OS heißt es jedoch, daß diese Arbeitsweise offensichtlich deshalb nicht angewendet wurde,
da die verfügbaren HCG-Antiseren komplexe Mischungen darstellen, die einen großen Anteil an anderen Bestandteilen als
HCG-Antikörper aus den Antiseren enthalten. In dieser
DT-OS wird ferner als weiterer Nachteil der Agglutiniertests
festgestellt,daß die Teilchen aus einer Reihe von Gründen agglomerieren können, die nichte mit einem immunologischen
Agglutinieren zu tun haben, wodurch die Verläßlichkeit der Testsvermindert wird.
7098? 1/09 10
26b1388 M
Eine Entdeckung, die in dieser DT-OS beschrieben wird, besteht darin, daß ein beliebiges Protein auf einem Substrat
nur in einer monomolekularen Schicht adsorbiert wird und daß sich ein spezifischer Antikörper (bzw. Antigen) für ein derartiges
beliebiges Protein mit dem Protein unter Bildung einer bimolekularen Proteinschicht auf dem Substrat verbindet.
Insbesondere kann eine Scheibe bzw. Oblate eines Substratmaterials in eine lösung eines ersten Proteins eingetaucht
werden, so daß eine monomolekulare Schicht des ersten Proteins am Substrat haftet. Das auf diese Weise überzogene Substrat
wird in eine zweite Lösung eingetaucht, die ein zweites Protein enthalten kann, das spezifisch mit dem ersten Protein
reagiert. Das zweite Protein (jedoch nur dieses Protein) bildet beim Vorliegen in der zweiten Lösung eine monomolekulare
Schicht auf der monomolekularen Schicht des ersten Proteins auf dem Substrat. Das überzogene Substrat wird nach
dem Eintauchen in die zweite Lösung elektrisch oder optisch untersucht, um festzustellen, ob eine bimolekulare oder monomolekulare
Schicht aus Protein anhaftet, wodurch angezeigt wird, ob die zweite Lösung tatsächlich das zweite Protein
enthält oder nicht.
Gemäß der Erfindung wird ein erstes Protein bzw. ein Antigen auf mikroskopischen [Teilchen aufgetragen. Derartige
Teilchen, die auf die angegebene Weise überzogen wurden,
zeigen eine bestimmte elektrophoretische Beweglichkeit.
Wenn ein Protein, das spezifisch mit dem ersten Protein
reagiert, z.B. ein Antikörper, danach mit dem ersten Protein in einer verdünnten Lösung des Antikörpers kombiniert
wird, fällt die elektrophoretische Beweglichkeit.der Teilchen
auf einen viel kleineren Wert ab, da die Antikörpermoleküle eine viel kleinere Beweglichkeit als die meisten anderen
Proteine beim normalen pH-Wert der Lösung besitzen. Durch geeignetes Einstellen des pH-Wertes erhält man einen wesentlichen
Beweglichkeitsunterschied zwischen den Antigenfilmen,
die als monomolekulare Schicht auf einigen Teilchen vorliegen, und den Antigen/Antikörper-Filmen, die als bimolekulare
Schicht auf anderen Teilchen vorliegen. Dieser Versuch zum
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Ermitteln einer Komplexbildung eignet sich zum Erzielen einer hohenEmpfÜndlLchkeit, da das Mischen der Lösung mit
einem G-ehalt an Teilchen und Antikörpern ein viel wirksamerer
Weg zur Herstellung eines Kontakts als das Inberührungbringen einer Proteinlösung mit einer ebenen makroskopischen Fläche ist.
Auch vermeidet die Ermittlung einer Molekülschichtbildung auf mikroskopischen Flächen die Unempfindlichkeit und andere
Probleme, die mit dem Ermitteln des Agglutinierens verbunden
sind. Als weiterer Vorteil kann ein wesentliches Überziehen der Teilchenflächen in 10 bis 20 min bei Proteinkonzentrationen
im Bereich von ng/cm erreicht werden, während bei makroskopischen
ebenen Flächen die Zeitspanne zum Erzielen eines vergleichbaren Überzugs bei derselben verdünnten Proteinkonzentration
etwa 10 h beträgt.
Gemäß einer bevorzugten Ausführungsform der Erfindung sieht eine Methode zum Ermitteln einer Antigen/Antikörper-Reaktion
als Stufen das Auftragen eines Antigens auf vielen mikroskopischen
Teilchen und die Bildung einer verdünnten Suspension der Teilchen in einer Lösung vor, die auf das Vorliegen von
Antikörpern geprüft werden soll, die für das Antigen auf den Teilchen spezifisch sind. Die Suspension wird gerührt und
die elektrophoretisch^ Beweglichkeit der Teilchen wird danach
gemessen.
Nachstehend wird die Erfindung näher erläutert, wobei
Figur 1 eine isometrische Ansicht einer Vorrichtung darstellt, die bei der Durchführung der Methode gemäß der Erfindung
verwendet werden kann.
Zu Vorbedingungen für dieEnpfindlichkeit der Ermittlungsmethode
gemäß der Erfindung gehören die Auswahl mikroskopischer Teilchen,
die mit einer monomolekularen Proteinschicht überzogen werden, die Teilchenkonzentration in der Lösung und die
Mischarbeitsweise. Teilchen, die Polystyrolkugeln mit einem
Durchmesser von 0,31 um darstellen und zum Entfernen von
oberflächenaktiven Stoffen und-anderen Verunreinigungen
dialysiert worden sind, sind erfolgreich verwendet worden.
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Jedoch ist die Erfindung nicht auf Polystyrolteilchen beschränkt,
da andere Teilchen, die Proteine adsorbieren, wie SiIiciumdioxidteilchen, gleichfalls brauchbar sind. Es
können die meisten kolloidalen Teilchen grundsätzlich brauchbar
sein, da keine Einschränkung hinsichtlich der Porm oder der Gleichmäßigkeit der Größe besteht, vorausgesetzt, daß
das spezifische Gewicht der Teilchen so gewählt wird, daß die Teilchen in Suspension mindestens einige Minuten lang
verbleiben, so daß die optischen Streumessungen ausreichend lange durchgeführt werden können. I1Ur eine ausreichendeEmpfindlichkeit
müssen die Testteilchenlösungen recht verdünnt sein, da der Gesamtteilchenoberflächenbereich klein gehalten
werden muß (z.B. viel kleiner als 1 cm ). Konzentrationen von 10 bis 10 Teilchen/cm , wobei die Teilchen einen Durchmesser
von 0,81yum besitzen, sind als befriedigend ermittelt
worden.
Eine hoheEnpÖndlidikeit muß nicht unbedingt vorteilhaft sein,
wenn sie von nicht-spezifischen Effekten begleitet ist, die
im allgemeinen in konzentrierten Seren- oder Proteinlösungen auftreten. In diesem 3?all reicht das Waschen der mikroskopischen
Teilchen durch Zentrifugieren aus, um nicht-spezifische
Beweglichkeitsveränderungen zu vermeiden, die sonst durch das Einwirken derartiger konzentrierter lösungen auf die
Teilchen auftreten wurden. Das Vorliegen der zweiten Proteinschicht
kann danach mit maximaler Enpfirrflichkeit ermittelt
werden, wenn sich die Kugeln in einer 0,005 η Natriumchloridlösung
beobachtet werden.
Das Mischen wurde unter Verwendung eines üblichen Magnetin tens ivr uhr er s in einem Becher und durch elektrophoretisches
Rühren in einer optischen Zelle durchgeführt. Das elektrophoretische Rühren ist besonders brauchbar, da es zu einer
Bewegung der mikroskopischen Teilchen in bezug auf die unmittelbar umgebende Flüssigkeit führt. Zum optimalen Mischen
kann es am günstigsten sein, turbulente und elektrophoretische Bewegung zu kombinieren, wobei die elektro-
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phoretische Bewegung ein ausreichend hohes elektrisches Feld erfordert, um die elektrophoretisch^ Bewegung zu
erzielen.
Die Technik zum Ermitteln einer Antigen/Antikörper-Kombination
auf einer mikroskopischen Oberfläche hängt von der Veränderung der elektrophoretischen Beweglichkeit der
Teilchen ab, die mit Protein beladen sind. Eine bestimmte elektrophoretisch^ Beweglichkeit hängt von einer Fläche ab,
die von einem Antigen auf einem Teilchen gebildet wird. Wenn man danach ein Antikörpermolekül mit dem Protein kombiniert,
fällt die Beweglichkeit des Teilchensauf einen viel kleineren Wert ab, da die Antikörpermoleküle eine
viel geringere Beweglichkeit als die meisten anderen Proteine beim normalen pH-Wert besitzen. Zusätzlich kann der pH-Wert
im Bereich von etwa 4-,O bis 8,0 eingestellt werden, so daß
eine wesentliche Beweglichkeitsdifferenz zwischen den Antigenund
Antigen/Antikörper-Filmen eingehalten wird. Die Beweglichkeit der mit Antigen überzogenen Teilchen ändert
sich um den Faktor 2 oder 3, wenn man Antikörpermoleküle mit dem Antigen kombiniert.
Die elektrophoretische Beweglichkeit wird durch die Messung
von Laserlicht gemessen, das von den Teilchen gestreut wird. Das gestreute Licht zeigt - infolge des Doppler-Effekts
und der elektrophoretischen Bewegung der Teilchen - eine Frequenzverschiebung, wenn ein elektrisches Feld an die
Teilchenlösung angelegt wird. Diese Art der Messung, axe
von E. E. Uzgiris in "Electrophoresis of Particles and
Biological Cells Measured by the Doppler Shift of Scattered Laser Light", Optics Communications 6 (September 1972) 55,
beschrieben wurde, ermöglicht es, daß selbst eine teilweise Bedeckung der Teilchenoberfläche mit Antikörpermolekülen
leicht beobachtet werden kann. Es kann eine wesentliche Teilchenoberflächenbedeckung nach 10 bis 20 min bei Proteinkonzentrationen
im Bereich von ng/cnr erhalten werden.
709821/0910
Ein optisches Doppler-Elektrophoresemeßsystem zum Ermitteln
von Beweglichkeitsveränderungen, wie sie in der vorstehenden
Veröffentlichung beschrieben werden, wird anhand der Figur erläutert. Das System umfaßt eine Elektrophoresezelle 10
mit einem Fluidbehälter 11 aus einem lichtdurchlässigen,
fluidundurchlässigen Material, beispielsweise Glas oder
Kunststoff. Ein Paar Elektroden 12 und 13 ist in der Zelle 10 eng nebeneinander angeordnet. Diese Elektroden weisen
vorzugsweise eine rechteckige Form auf und besitzen jeweils sich parallel gegenüberliegende Flächen, die einen Spalt
zwischen den Elektroden begrenzen, dessen Breite nicht 1 mm überschreitet.
Der Behälter 11 ist mit einer verdünnten kolloidalen Suspension gefüllt, die mikroskopische Teilchen mit einer Schicht
aus darauf adsorbiertem Protein enthält; es wird ein elektrisches Feld zwischen den Elektroden 12 und 13 durch die
Stromversorgung 14 angelegt. Der Spalt zwischen den Elektroden 12 und 13 wird durch kohärente optische Energie
eines Lasers 15 erleuchtet. Ein Teil dieser Energie wird
durch die mikroskopischen Teilchen im Spalt zwischen den Elektroden 12 und 13 gestreut und zeigt infolge der Bewegung
der streuenden Teilchen im elektrischen Feld - eine Doppler-Frequenzverschiebung. Die in einem vorgegebenen
Winkel gestreute Energie wird von einem optischen Anzeigegerät 16 empfangen, vorzugsweise einem Photoverstärkerrohr;
es kann sich jedoch um irgendeinen geeigneten quadratischen Gleichrichter handeln.
Die Anzeigevorrichtung 16 empfängt infolge des Doppier-Effekts verschobene Energie, die von den Teilchen in der
Suspension im Fluidium im Innern des Behälters 11 gestreut wird, und ferner nicht verschobene Energie , die von
festen streuenden Objekten gestreut wird, z.B. der Wandung des Behälters 11.Da die Anzeigevorrichtung 16 sowohl infolge
des Doppler-Effekts verschobene als auch unverschobene
Energie aufnimmt und ein quadratischer Gleichrichter ist, ist ihr abgegebenes Signal ein Maß für das überlagsrungs-
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Produkt der beiden empfangenen Frequenzen; es kann daher
nach üblichen Arbeitsweisen zur Bestimmung der elektrophoretischen Beweglichkeit der Teilchen in der Zelle 10
zu zwei verschiedenen Zeitpunkten analysiert werden, um eine Verminderung der Beweglichkeit zu ermitteln, die zwischen
diesen beiden Zeitpunkten eingetreten sein kann.
Vorstehend wird eine Methode zum raschen Ermitteln eines spezifischen Proteins in einer Lösung beschrieben. Die
Methode ist sowohl einfach als auch hoch empfindlich und läßt die Ermittlung der Bildung diskreter Molekülschichten von
Proteinen zu. Es können spezifische Immunreaktionen sensitiv nach dieser Methode ermittelt werden.
709821/0910
Leerseite
Claims (5)
1. Verfahren zum Ermitteln einer Reaktion zwischen einem ersten Protein bzw. einem Antigen und einem zweiten Protein
bzw. einem Antikörper, dadurch gekennzeichnet, daß man das erste Protein bzw. das Antigen auf vielen mikroskopischen
Teilchen aufträgt, eine verdünnte Suspension der Teilchen in einer Lösung bildet, die auf das Vorliegen des zweiten
Proteins bzw. des für das Antigen spezifischen Antikörpers getestet werden soll, die Suspension rührt und die elektrophoretische
Beweglichkeit bzw. deren Verminderung der Teilchen ermittelt.
2. Verfahren nach Anspruch 1, dadurch gekennzeichnet,
daß man die Lösung durch elektrophoretische Bewegung mischt.
3. Verfahren nach Anspruch 1 oder 2, dadurch gekennzeichnet, daß man die Lösung turbulent und durch elektrophoretische
Bewegung mischt.
4. Verfahren nach einem der vorhergehenden Ansprüche, dadurch gekennzeichnet, daß man die Beweglichkeit der
Teilchen mißt, indem man die Beweglichkeit der Teilchen zu zwei verschiedenen Zeitpunkten vergleicht.
5. Verfahren nach Anspruch 4, dadurch gekennzeichnet, daß man zum Vergleich der Beweglichkeiten der Teilchen
zu zwei verschiedenen Zeitpunkten unter einem vorgegebenen Streuwinkel Laserlicht, das von den Teilchen und von einem
festen Lichtstreugegenstand gestreut wird, zu jedem der beiden verschiedenen Zeitpunkte auffängt, das Überlagerungs-Produkt
der Frequenzen analysiert, die zu jedem der beiden verschiedenen Zeitpunkte ermittelt wurden, und die analysierten
Überlagerungs-Produktejvergleicht und ein Maß für
die veränderte Beweglichkeit der Teilchen zwischen den beiden Zeitpunkten erhält.
ORIGINAL
709821/0910
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US05/631,727 US3984533A (en) | 1975-11-13 | 1975-11-13 | Electrophoretic method of detecting antigen-antibody reaction |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DE2651388A1 true DE2651388A1 (de) | 1977-05-26 |
Family
ID=24532483
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE19762651388 Withdrawn DE2651388A1 (de) | 1975-11-13 | 1976-11-11 | Verfahren zur ermittlung einer antigen-antikoerper-reaktion oder protein/protein-reaktion |
Country Status (5)
| Country | Link |
|---|---|
| US (1) | US3984533A (de) |
| JP (1) | JPS5270018A (de) |
| DE (1) | DE2651388A1 (de) |
| FR (1) | FR2331793A1 (de) |
| GB (1) | GB1542493A (de) |
Families Citing this family (861)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IT1055851B (it) * | 1974-08-30 | 1982-01-11 | Behringwerke Ag | Particelle indicatirci per diagnosi in vitro |
| US3984533A (en) * | 1975-11-13 | 1976-10-05 | General Electric Company | Electrophoretic method of detecting antigen-antibody reaction |
| US4080264A (en) * | 1976-03-01 | 1978-03-21 | Massachusetts Institute Of Technology | Immunoassay by light scattering spectroscopy |
| JPS5811575B2 (ja) * | 1976-08-16 | 1983-03-03 | 帝国臓器製薬株式会社 | 抗原−抗体反応の測定法 |
| US4208185A (en) * | 1976-08-16 | 1980-06-17 | Mitsubishi Chemical Industries Limited | Method and apparatus for the measurement of antigens and antibodies |
| US4203724A (en) * | 1976-08-16 | 1980-05-20 | Mitsubishi Chemical Industries Limited | Method and apparatus for the measurement of antigens and antibodies |
| US4154669A (en) * | 1977-02-11 | 1979-05-15 | Pen Kem, Inc. | Automatic electrophoresis apparatus |
| US4101220A (en) * | 1977-03-31 | 1978-07-18 | General Electric Company | Laser Doppler spectroscopy with smoothened spectra line shapes |
| US4171956A (en) * | 1977-06-13 | 1979-10-23 | General Electric Company | Laser immunoassay |
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| US3091697A (en) * | 1955-03-03 | 1963-05-28 | Ethel D Armbrecht | Photomultiplier control circuit |
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| BE789188A (fr) * | 1971-09-24 | 1973-01-15 | Orion Yhtymae Oy | Procede pour la determination quantitative et qualitative de molecules ayant des proprietes antigenes |
| US3732014A (en) * | 1972-01-31 | 1973-05-08 | Gen Electric | Electromagnetic radiation apparatus for analyzing small particles |
| US3819505A (en) * | 1972-03-09 | 1974-06-25 | Becton Dickinson Co | Testing apparatus |
| US3793180A (en) * | 1972-03-21 | 1974-02-19 | Singer Co | Laser-recticle electrophoresis instrument |
| US3764512A (en) * | 1972-05-02 | 1973-10-09 | Singer Co | Laser scanning electrophoresis instrument and system |
| US3873432A (en) * | 1972-10-30 | 1975-03-25 | Louis Israel | Continuous preparative electrophoresis method |
| US3766048A (en) * | 1972-11-24 | 1973-10-16 | Univ Illinois | Analysis of polymer mixtures in solution utilizing electrophoretic light scattering apparatus |
| US3912610A (en) * | 1974-07-23 | 1975-10-14 | Icl Scient | Method for electroquantitative determination of proteins |
| US3984533A (en) * | 1975-11-13 | 1976-10-05 | General Electric Company | Electrophoretic method of detecting antigen-antibody reaction |
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1976
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- 1976-11-12 JP JP51135441A patent/JPS5270018A/ja active Pending
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|---|---|
| FR2331793A1 (fr) | 1977-06-10 |
| GB1542493A (en) | 1979-03-21 |
| FR2331793B1 (de) | 1981-12-24 |
| JPS5270018A (en) | 1977-06-10 |
| US3984533A (en) | 1976-10-05 |
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