American Society of Hematology

Fig. 2.

$Fig. 2. Activity of vWF-cleaving protease in fractions eluted from Sephacryl S-300 HR. / (A) SDS-agarose gel electrophoresis of unreduced vWF substrate after incubation with chromatographic fractions eluted from Sephacryl S-300 HR. Disappearance of high-molecular-weight vWF multimers is indicative of vWF-cp activity. (B) SDS-PAGE of reduced vWF substrate after incubation with citrated normal plasma diluted 1:20 (lane b) or with a 4-fold concentrated pool of purified vWF-cp preparation (lane c). The vWF subunit is completely degraded to fragments of 170 and 140 kd. The protease-free control in lane a contains only the undegraded vWF subunit of 250 kd.$

Activity of vWF-cleaving protease in fractions eluted from Sephacryl S-300 HR.

(A) SDS-agarose gel electrophoresis of unreduced vWF substrate after incubation with chromatographic fractions eluted from Sephacryl S-300 HR. Disappearance of high-molecular-weight vWF multimers is indicative of vWF-cp activity. (B) SDS-PAGE of reduced vWF substrate after incubation with citrated normal plasma diluted 1:20 (lane b) or with a 4-fold concentrated pool of purified vWF-cp preparation (lane c). The vWF subunit is completely degraded to fragments of 170 and 140 kd. The protease-free control in lane a contains only the undegraded vWF subunit of 250 kd.

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