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Fig. 6 | BMC Biochemistry

Fig. 6

From: A comparison of the enzymatic properties of three recombinant isoforms of thrombolytic and antibacterial protein—Destabilase-Lysozyme from medicinal leech

Fig. 6

Fibrinolytic activity of mlDL-Ds3. a Lysed zone formation in the fibrin plate after treatment with the intact entire mlDL-Ds3. 1—mlDL-Ds3, 2—mlDL-Ds3t, 3—heat-inactivated mlDL-Ds3. bSDS-PAGE of fibrin gel lysed by mlDL: 1–probe from mlDL lysed zone, 2–soluble fraction of stabilized fibrin by 2 % acetic acid treatment, 3–unsoluble fraction of stabilized fibrin by 2 % acetic acid treatment, (c) SDS-PAGE of stabilized fibrin after mlDL-Ds3 treatment at 37 °C for 96 h: 4—unsoluble fraction of stabilized fibrin after incubation with control buffer, 5—unsoluble fraction of stabilized fibrin after incubation with mlDL-Ds3, 6—soluble fraction of stabilized fibrin after incubation with control buffer, 7—soluble fraction of stabilized fibrin after incubation with mlDL-Ds3, 8—mlDL-Ds3. M—molecular weight marker (kDa). Electrophoresis was performed in 12 % acrylamide/bis gel. The gel was stained with Coomassie 250G. α, β, γ—α, β, γ-chains of human fibrinogen (63.5, 56, 47 kDa respectively)

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