Key result
A simple method for ECP32 preparation and storage was developed, yielding purity and activity levels that satisfy the requirements for actin structure and function investigations.
A new, simple method for the preparation and storage of protease ECP32 was developed to facilitate investigations of actin structure and function.
Simplifies ECP32 prep for actin studies; leaves open translation to human cardiovascular models.
The protease ECP32 is significant in investigations of actin, the basic protein of muscles and the cytoskeleton. The enzyme originates from the natural enterobacteria strain, which accumulates minor amounts of the protease intracellularly at the post-exponential growth phase. The limiting factor for biosynthesis is the amount of oxygen that has entered the medium. The highly effective method of two-phase cultivation with vigorous aeration at the exponential growth phase was recommended. Based upon the enzyme properties studied, there is a decreased potential for success when using either the affinity or one-stage purification methods. In order to overcome obstacles in the aforementioned methods, a simple method for ECP32 preparation and storage was developed, with purity and activity levels satisfying the requirements of actin structure and function investigations.
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Morozova et al. (2009) studied this question. Express-method of obtaining protease ECP32 was evaluated on Purity and activity levels of ECP32 preparation. A simple method for ECP32 preparation and storage was developed, yielding purity and activity levels that satisfy the requirements for actin structure and function investigations.
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