EC Number   |
Reference |
|---|
    3.1.8.1 | - |
35219 |
| 3.1.8.1 | activity lost during incubation in phosphate buffer can be restored by addition of CoSO4 or CuSO4 |
646542 |
| 3.1.8.1 | refolding of recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) inclusion bodies. The recombinant proteins are refolded to their active form by in vitro refolding, and the active protein present in the refolding reaction mixture is further purified |
749628 |
| 3.1.8.1 | refolding of recombinant wild-type and mutant enzymes from inclusion bodies in Escherichia coli strain BL21(DE3) by 8 M urea |
751939 |
| 3.1.8.1 | the conformational stability of SsoPox against the denaturing action of guanidine-HCl has been investigated at 25°C, pH 8.0, 20 mM TrisHCl buffer, by performing CD and fluorescence measurements. The transition curves obtained by recording the molar ellipticity at 222 nm (detecting the secondary structure stability) present two inflection points, at 2.6 M guanidine-HCl and about 4.8 M guanidine-HCl, respectively, with a plateau at about 3 M guanidine-HCl. SsoPox is markedly more resistant to the denaturing action of guanidine-HCl with respect to the mesophilic counterpart. Overall guanidine-HCl-induced denaturation of SsoPox is not a reversible process in all the investigated experimental conditions: upon suitable dilution of fully denatured samples, there is not a complete recovery of the far-UV CD spectrum or fluorescence emission spectrum of the native enzyme |
719426 |
| 3.1.8.1 | the inactive recombinant His6-tagged wild-type and mutant enzymes present in the inclusion bodies in Escherichia coli strain BL21(DE3) are refolded to their active form using in vitro refolding, best from refolding buffer containing 200 mM TAPS, pH 8.5, 1.0 M NDSB 201, 1 mM EDTA, 2.2 mM GSH, 0.22 mM GSSH, and 10 mM CaCl2, method optimization, overview. The catalytic properties of the refolded enzymes are similar to their soluble counterparts. The extent of refolding of rh-PON1 is more when 8 M urea is used as a chaotropic agent to denature the rh-PON1 present in inclusion bodies, low concentration of rh-PON1 protein (0.005 mg/ml) is used in the refolding reaction, and when the refolding reaction is incubated for 12 h at 25°C, but low concentration of protein in in vitro refolding is generally not economical for large-scale production of protein, thus 0.020 mg/ml protein concentration is selected for the refolding reaction |
752094 |
