Method of separating protein aggregate in mixed liquid of denatured protein/incusion protein renaturation
A technology for protein aggregates and protein refolding, which is applied in the field of separation of protein aggregates in the denatured protein/inclusion body protein refolding mixture, which can solve the problems of inability to separate components, complex protein components, and difficult separation of various components
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Embodiment 1
[0018] Embodiment 1: Separating the protein aggregates in the denatured natural chicken egg white lysozyme protein refolding mixture to obtain a single-component natural chicken egg white lysozyme protein, the steps are as follows:
[0019] 1. Collect the natural chicken egg white lysozyme protein mixture after refolding, which contains correctly folded and refolded proteins, unfolded or misfolded proteins, and protein aggregates;
[0020] 2. Separation of protein aggregates in the natural chicken egg white lysozyme protein mixture after refolding
[0021] 1) Add 0.15 mol / L NaCl and 2 mol / L urea to 0.1 mol / L Tris-HCl, pH 8.7 gel filtration chromatography buffer to prepare a solution containing 0.15 mol / L NaCl and 2 mol / L The gel filtration chromatography buffer of urea of L: and equilibrate Superdex 75 (10 / 30) gel filtration chromatography column with this buffer;
[0022] 2) Put the collected natural chicken egg white lysozyme protein mixture into the column, and use the a...
Embodiment 2
[0024] Example 2: The natural chicken egg white lysozyme protein after refolding was eluted with a buffer containing denaturant and salt ions, and the formation of refolded protein components was studied using a buffer without denaturing agents and salt ions as a control :
[0025] The gel filtration chromatography column used is a Superdex 75 prepacked column, and the elution flow rate is 0.4mL / min. figure 2 Curve 1 in the figure is: when the natural chicken egg white lysozyme protein after refolding was eluted using the gel filtration chromatography buffer solution without denaturing agent and salt ion, it was found that there was only one elution peak (the peak after the ion was peak), and the peak time is relatively late, suggesting that adsorption has occurred between the components of the three peaks and with the chromatographic column;
[0026]When the gel filtration chromatography buffer used contains a low concentration of NaCl, when the concentration of urea in the...
Embodiment 3
[0029] Example 3, using Tris-HCl buffer solution containing 1.5mol / L guanidine hydrochloride and 0.1mol / L potassium carbonate (or 0.1mol / L potassium acetate) to elute the protein in the mixed solution after human lysozyme inclusion body refolding Aggregate, make the natural chicken egg white lysozyme protein of single component, can obtain the similar separation effect with embodiment 1.
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