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The rMCP7 was purified via an ammonium sulfate precipitation, using casein as a carrier protein, followed by cation exchange chromatography.
Similar experiments were performed for measuring protease activity using casein as a substrate.
Proteolytic activity of CPE was determined using casein as a substrate according to the method of An et al. (1994).
With the exception of Hp1019, we did not detect any proteolytical activities using casein as a substrate in zymography studies (data not shown).
Protease activity was visualized by in-gel assays using casein as a substrate [ 45].
Purified PvNod41 was tested for activity using casein as a substrate in 50 mM sodium citrate, pH 4.5 at 37°C.
Similar(50)
Therefore, we used casein as a substrate in the subsequent experiments to study the biochemical properties of BbKst-kinase.
We additionally used casein as an artificial substrate for HtrA [32] leading to similar results (Figure 2B).
Based on Mechakra et al. 1999 method, a proteolytic activity assay was done using casein as the substrate.
Activity staining of ATPS fractions by using casein as substrate was shown in Figure 5B.
Enzyme activity was measured daily by the modified method of Anson (Anson 1938) using casein as substrate.
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