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Original

Immobilization of Glutathione-s-transferase Within Cross-Linked Gelatin Cylindrical Molds

Pages 47-57 | Published online: 24 Aug 2009

Figures & data

Table 1. Effect of enzyme, gelatin and formaldehyde concentration on the immobilization efficiency of cytosolic GST preparation by means of activity yield

Figure 1. The effect of pH on the activity of free(▪) and immobilized(•) GST activity (sodium acetate; pH 3.0–6.0, phosphate; pH 6.5–7.5, borate; pH 8.0–9.0).

Figure 1. The effect of pH on the activity of free(▪) and immobilized(•) GST activity (sodium acetate; pH 3.0–6.0, phosphate; pH 6.5–7.5, borate; pH 8.0–9.0).

Figure 2. The effect of Temperature on the activity of free(▪) and immobilized(•) GST activity.

Figure 2. The effect of Temperature on the activity of free(▪) and immobilized(•) GST activity.

Figure 3. Thermal Stability of free(▪) and immobilized(•) GST.

Figure 3. Thermal Stability of free(▪) and immobilized(•) GST.

Figure 4. Quantities of 2,4‐dinitrophenyl‐GSH in a stirred batch reaction of glutathione conjugation.

Figure 4. Quantities of 2,4‐dinitrophenyl‐GSH in a stirred batch reaction of glutathione conjugation.

Figure 5. Conversion curve of CDNB in a batch reactor system (So→30 μmol).

Figure 5. Conversion curve of CDNB in a batch reactor system (So→30 μmol).

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