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Kinetic studies on the oxidation of nitrite by horseradish peroxidase and lactoperoxidase

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Gębicka L.
Acta Biochimica Polonica
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1999
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vol. 46
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issue 4
919-927
EN
The reaction of nitrite (NO-_2) with horseradish peroxidase and lactoperoxidase was studied. Sequential mixing sopped-flow measeruments gave the following values for the rate constants of the reaction of nitrite with compounds II (oxoferryl heme intermediates) of horseradish peroxidase and lactoperoxidase at pH 7.0, 13.3 ± 0.07 mol^{-1}dm^3s^{-1} and 3.5 ± 0.05 · 10^4mol^{-1}dm^3s^{-1}, respectively. Nitrite, at neutral pH, influenced measurements of activity of lactoperoxidase with typical substrates like 2,2'-azino-bis[ethyl-benzothiazoline-(6)-sulphonic acid] (ABTS), guaiacol or thiocyanate (SCN-). The rate of ABTS and guaiacol oxidation increased linearly with nitrite concentration up to 2.5-5 mmol dm^{-3}. On the other hand, two-electron SCN- oxidation was inhibited in the presence od nitrite. Thus, nitrite competed with the investigated substrates of lactoperoxidase. The intermediate, most probably nitrogen dioxide (*NO_2), reacted more rapidly with ABTS or guaiacol than did lactoperoxidase compound II. It did not, however, effectively oxidize SCN- to OSCN-. NO-_2 did not influence the activity measurements of horseradish peroxidase by ABTS or guaiacol method.
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Controllable preparation of highly active horseradish peroxidase-gold nanoparticle bionanoconjugate

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Zhang P., Liu C., Song S., Peng C.
Polish Journal of Chemical Technology
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2012
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vol. 14
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issue 4
57-60
EN
A novel method of immobilizing horse radish peroxidase enzyme (HRP) onto the surface of gold nanoparticles (GNPs) was developed. As a result, a high-activity bionanoconjugates was obtained through utilizing the biotin-streptavidin (SA) system. The HRP-SA-GNP bionanoconjugate with high activity was conveniently prepared through the biotin- avidin system. Compared with the HRP-GNP bioconjugate prepared through the traditional electrostatic absorption method, the enzyme activity per GNPs of this new bionanoconjugate was enhanced by 10 times. Moreover, the enzyme activity of this bionanoconjugate was controllable. The above method of bionanoconjugation preparation has promising applications in the fields including preparing highly active bio-nanoprobe and immobilized enzyme.
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