ES2554162T3 - Método para determinar la actividad del factor de von Willebrand en ausencia de ristocetina - Google Patents

Método para determinar la actividad del factor de von Willebrand en ausencia de ristocetina Download PDF

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ES2554162T3
ES2554162T3 ES08773827.4T ES08773827T ES2554162T3 ES 2554162 T3 ES2554162 T3 ES 2554162T3 ES 08773827 T ES08773827 T ES 08773827T ES 2554162 T3 ES2554162 T3 ES 2554162T3
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ristocetin
von willebrand
willebrand factor
gpibα
absence
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Harald Althaus
Tobias Obser
Juergen Patzke
Reinhard Schneppenheim
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Siemens Healthcare Diagnostics Products GmbH
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Abstract

Método para la determinación de la actividad del factor de von Willebrand (VWF) en una muestra, en el cual la muestra se mezcla con una proteína GPIbⲁ aislada para producir una preparación de ensayo, el cual está caracterizado porque a) se utiliza proteína GPIbα aislada, la cual comprende una secuencia de aminoácidos que en comparación con la secuencia de tipo silvestre de la proteína GPIbα humana (SEQ ID NO:1) contiene al menos los residuos de aminoácidos 1-268 y presenta una sustitución de aminoácidos Xaa en las posiciones 233 y 239, respectivamente, y porque b) a la preparación de ensayos no se adiciona ristocetina ni botrocetina y porque c) la proteína GPIbα utilizada está asociada con una fase sólida en forma de partículas.

Description

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1) descongelamiento de las células (1 Kryo con 5-10x 10e6 células) y cultivo en T175 en medio que contiene suero durante 96h
2) dividir en 4x T175 y cultivo durante 72-96h
3) dividir en 25x T175 y cultivo durante 72-96h
4) dividir una T175 y seguir cultivando como reserva. Dividir las restantes 24x T175 en 3x CellStack Corning (de a 10 niveles de CellStack en total con 6360cm2) y cultivar durante 72h
5) retirar medio monocapa con DMEM sin FBS 1-2x lavar y adicionar OPTIPRO-SFM libre de suero (1,8 litros por CellStack) y cultivar durante 96h
6) cosecha del medio. Centrifugar sobrenadante y recuperar el comprimido de las células desprendidas y devolverlas al CellStack con OPTIPRO-SFM recién hecho y cultivar durante 96h
7) tal como en 6)
8) cosecha final del medio y finalización del cultivo
Ejemplo 3: aislamiento por cromatografía de afinidad de la proteína de fusión-GPIbα-(G233V/M239V)-(33Flag)(63His)
El medio que contiene GPIbα-(G233V/M239V)-(3xFlag)-(6xHis) obtenida según el ejemplo 2 se libera de las células
o de partes de la ruptura de células aún presentes mediante centrifugación (35 min, 10.000 rpm, Beckman J2-21, Beckman Coulter GmbH, Alemania). El sobrenadante libre de células, obtenido de esta manera, se concentra por medio de ultrafiltración tangencial usando un casete de ultrafiltración con un límite de separación de 10 kDa (PES 10, Schleicher & Schüll, Alemania) a 1/10 del volumen de partida.
La purificación se efectúa por medio de cromatografía de afinidad usando una Ni2+-Sefarosa (His Prep FF16/10, GE Healthcare, Suecia) según las indicaciones del fabricante. Para enlazar la GPIbα-(G233V/M239V)-(33Flag)-(63His) al sobrenadante concentrado se adicionan NaCl de 500 mmol, Na2HPO4 de 20 mmol e imidazol de 5 mM y adicionando HCl de 5 M se ajusta el valor de pH a 7,4. Los componentes no enlazados se retiran lavados enjuagando la columna con un regulador de pH hecho de NaCl de 500 mmol, Na2HPO4 de 20 mmol, imidazol de 5 mM, pH 7,4. La elución de la GPIbα-(G233V/M239V)-(33Flag)-(6xHis) enlazada se efectúa con un regulador de pH hecho de Na2HPO4 de 20 mmol, NaCl de 500 mmol, imidazol de 500 mMol, pH 7,4. El material eluido obtenido de esta manera se concentra en una celda de ultrafiltración con agitación, con una membrana de ultrafiltración, límite de separación de 10 kDa (OMEGA 10 K, Pall Life Sciences, USA) a 1/10 del volumen de partida. La otra purificación y separación de contaminantes se efectúa por medio de filtración en gel usando una columna de cromatografía Superdex 200 grado preparativo 35/600 (GE Healthcare, Suecia) de acuerdo con indicaciones del fabricante. La cromatografía se efectúa con una tasa de flujo de 5,0 ml/min usando un regulador de pH hecho de Na2HPO4 de 0,048 mol/L, KH2PO4 de 0,02 mol/L, NaCl de 0,145 mol/L, NaN3 de 0,015 mol/L, pH 7,2. Después de cargar la muestra, GPIbα-(G233V/M239V)-(33Flag)-(63His) se eluye en un pico después de un volumen de elución de alrededor de 300 ml de la columna de cromatografía empleada.
Ejemplo 4: (no es parte de la invención): método para determinar la actividad de VWF en un anti-FLAG/GPIbα-ELISA sin ristocetina
Se utilizaron placas de ELISA, las cuales ya estaban recubiertas con un anticuerpo contra la etiqueta Flag-Tag (Sigma, Saint Louis, Estados Unidos, ANTI-FLAG HS, M2 coated 96-well Plates (clear), número de producto P 2983). En cada cavidad de la placa de ELISA se colocaron 100 µL de una solución de regulador de pH a base de fosfato, que contenía proteína de fusión -GPIbα-(33Flag)-(63His) de tipo silvestre recombinante (sobrenadante del medio de cultivo diluido 1:10 después de la sedimentación de las células) o proteína de fusión GPIbα-(aa1-285,G233V/M239V)-(33Flag)-(63His) recombinante aislada (véase Ejemplo 3) en una concentración de 2,4 mg/mL, y fue incubada por una noche a 2-8 °C. Después de lavar 4 veces con regulador de pH a base de fosfato (+ 0,01 % Tween®) se adicionaron 50 µl de una dilución de Hämate® (ZLB Behring, Marburg, Alemania) en regulador de pH a base de fosfato + 0,1 % del albúmina de suero bovino, así como 50 µl de una opción de ristocetina en regulador de pH de fosfato + 0,1 % de albúmina de suero bovino. Después se efectuó una incubación por 1 hora a temperatura ambiente. Después de lavar 4 veces tal como anteriormente, se adicionaron 100 µl de un anticuerpo anti-VWF acoplado a peroxidasa de rábano picante (horseraddish) (Rabbit Anti-Human VWF/HRP, DAKO, Ref. P0226), se incubó por 1 hora a temperatura ambiente y después se lavó tal como anteriormente. A continuación se adicionaron 100 µl de solución de tetrametilbencidina en calidad de sustrato (sustrato de TMB, Dade Behring Marburg GmbH, Marburg, Alemania, Ref. 450684). Se incubó por 4 minutos a temperatura ambiente. Adicionando 100 µl de ácido sulfúrico de 0,5 N se detuvo la reacción. Después se efectuó la medición de la extinción a 405 nm en un espectrofotómetro.
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Claims (1)

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ES08773827.4T 2007-07-06 2008-07-03 Método para determinar la actividad del factor de von Willebrand en ausencia de ristocetina Active ES2554162T3 (es)

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DE102007031708 2007-07-06
DE102007031708A DE102007031708A1 (de) 2007-07-06 2007-07-06 Bestimmung der von Willebrand Faktor-Aktivität in Abwesenheit von Ristocetin
PCT/EP2008/005416 WO2009007051A2 (de) 2007-07-06 2008-07-03 Verfahren zur bestimmung der von willebrand faktor-aktivität in abwesenheit von ristocetin und zur bestimmung der adamts-13-protease

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ES11002342T Active ES2425797T3 (es) 2007-07-06 2008-07-03 Métodos para la determinación de la actividad de escisión del factor de von Willebrand de la proteasa ADAMTS-13
ES08773827.4T Active ES2554162T3 (es) 2007-07-06 2008-07-03 Método para determinar la actividad del factor de von Willebrand en ausencia de ristocetina

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EP (2) EP2167978B1 (es)
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CN (3) CN101755211A (es)
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CA (2) CA2938781C (es)
DE (1) DE102007031708A1 (es)
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US20130078652A1 (en) 2013-03-28
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