22.214.171.124: bromide peroxidase
This is an abbreviated version!
For detailed information about bromide peroxidase, go to the full flat file. Reaction
apobromoperoxidase I, BPO, BPO 1, BPO 2, BPO I, BPO-A1, BPO-A2, BPO1, bromoperoxidase, bromoperoxidase A2, bromoperoxidase I, bromoperoxidase-catalase, BrPO, CoVBPO, CVBPO, EC 126.96.36.199, non-haem bromoperoxidase, non-haem bromoperoxidase BPO 1, non-haem bromoperoxidase BPO 2, non-haem bromoperoxidase BPO-A2, non-heme haloperoxidases, non-heme-type bromoperoxidase, nonhaem-type bromoperoxidase BPO 1a, nonhaem-type bromoperoxidase BPO 1b, nonhaem-type bromoperoxidase BPO 3, nonheme bromoperoxidase, nVBPO, rVBPO, sVBPO, V-BPO, V-BrPO, vanadate-dependent bromoperoxidase I, vanadium bromoperoxidase, vanadium containing bromoperoxidase, vanadium-containing bromoperoxidase, vanadium-dependent bromoperoxidase, vanadium-dependent bromoperoxidase 2, vanadium-dependent haloperoxidase, vanadium-dependent peroxidase, vBPO, VBPO1, VBPO2, VBrPO(AnI)
General Stability on EC 188.8.131.52 - bromide peroxidase
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activity half-life times increase along the series of buffers: phosphate -
after treatment with a mixture of chloroform/ethanol the enzyme still shows 65% of its initial brominating activity
Ca2+ significantly increased the enzyme stability. Strontium and magnesium ions have similar effects
circular dichroism measurements showed that the secondary structure is not affected upon incubation in 4% SDS
denaturation did not occur upon incubation in 4 M guanidine hydrochloride
dialysis of the enzyme preparation against 1 mM EDTA in 0.1 M citrate-phosphate buffer (pH 3.8) results in loss of enzymic activity. Incubation with vanadium, does not restore the enzymic activity. Also various other metal ions: Zn(II), Fe(II), Cu(II) and Mn(II) are ineffective in the reactivation of the preparation
vanadate increases the thermostability