I am currently purifying a protein (hGH-22.13 kDa). At first it was fusion protein and has His-tag and sumo as ubiquitin. The stages of purification are Ni-NTA, G25, digestion to remove His-tag and sumo, Ni-NTA to collect mature hGH in flowthrogh, TFF for exchanging buffer and finally Q-sepharose for fractionation.
The specification of fraction is (95% ≤native protein, 97%≤monomer, HCP ≤100 ng/mg, HCDNA≤10pg/dose, ) in ( 20 mM tirs, 5 mM methionine, 10 mM argenine, 100mM glycine, 20mM NaCL in pH 6.5) but it was not colorless also it is a little bit turbid with yellow color. What is the reason of this phenomena? Could anyone help me regarding this question to eliminate turbidity and color by use of some filtration system or adding some chemical or biological agent?
Regards
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