[Horseradish peroxidase: a study of the kinetics and the determination of optimal reaction conditions, using hydrogen peroxide and 2,2'-azinobis 3-ethylbenzthiazoline-6-sulfonic acid (ABTS) as substrates (author's transl)] - PubMed (original) (raw)
[Article in German]
- PMID: 33227
[Horseradish peroxidase: a study of the kinetics and the determination of optimal reaction conditions, using hydrogen peroxide and 2,2'-azinobis 3-ethylbenzthiazoline-6-sulfonic acid (ABTS) as substrates (author's transl)]
[Article in German]
H Gallati. J Clin Chem Clin Biochem. 1979 Jan.
Abstract
The reaction of the two substrates hydrogen peroxide and ABTS with horseradish peroxidase was studied kinetically. Enzyme activity was determined as a function of substrate concentration and pH. Michaelis constants were determined for the two substrates at various pH values. It was found that the affinity of the enzyme for ABTS decreases with increasing pH, and that with higher ABTS concentrations the pH optima of the reaction are shifted towards neutrality. Maximal rate is reached at pH 4.2 with an ABTS concentration of 2 mmol/l. For hydrogen peroxide the data show that the dissociated O2H- is the proper substrate, its affinity for the enzyme being independent of pH. The two substrates show competitive binding to the peroxidase, and each therefore influences the binding constant of the other. A procedure is proposed which allows the determination of peroxidase down to a concentration of 10 ng/l or 2.5 x 10(-13) mol/l.
Similar articles
- pH dependence and structural interpretation of the reactions of Coprinus cinereus peroxidase with hydrogen peroxide, ferulic acid, and 2,2'-azinobis.
Abelskov AK, Smith AT, Rasmussen CB, Dunford HB, Welinder KG. Abelskov AK, et al. Biochemistry. 1997 Aug 5;36(31):9453-63. doi: 10.1021/bi970387r. Biochemistry. 1997. PMID: 9235990 - Kinetic studies on the oxidation of nitrite by horseradish peroxidase and lactoperoxidase.
Gebicka L. Gebicka L. Acta Biochim Pol. 1999;46(4):919-27. Acta Biochim Pol. 1999. PMID: 10824860 - [Enzyme kinetics for enzyme immunoassay].
Sudo K. Sudo K. Nihon Rinsho. 1995 Sep;53(9):2134-9. Nihon Rinsho. 1995. PMID: 7474370 Review. Japanese.
Cited by
- Ultrasensitive detection of cancer biomarkers in the clinic by use of a nanostructured microfluidic array.
Malhotra R, Patel V, Chikkaveeraiah BV, Munge BS, Cheong SC, Zain RB, Abraham MT, Dey DK, Gutkind JS, Rusling JF. Malhotra R, et al. Anal Chem. 2012 Jul 17;84(14):6249-55. doi: 10.1021/ac301392g. Epub 2012 Jul 3. Anal Chem. 2012. PMID: 22697359 Free PMC article. - Aerotolerant Thiosulfate-Reducing Bacterium Fusibacter sp. Strain WBS Isolated from Littoral Bottom Sediments of the White Sea-Biochemical and Genome Analysis.
Brioukhanov AL, Kadnikov VV, Beletsky AV, Savvichev AS. Brioukhanov AL, et al. Microorganisms. 2023 Jun 23;11(7):1642. doi: 10.3390/microorganisms11071642. Microorganisms. 2023. PMID: 37512815 Free PMC article. - A Complex of LaoA and LaoB Acts as a Tat-Dependent Dehydrogenase for Long-Chain Alcohols in Pseudomonas aeruginosa.
Panasia G, Drees SL, Fetzner S, Philipp B. Panasia G, et al. Appl Environ Microbiol. 2021 Jul 27;87(16):e0076221. doi: 10.1128/AEM.00762-21. Epub 2021 Jul 27. Appl Environ Microbiol. 2021. PMID: 34085859 Free PMC article. - Histone H1 in two subspecies of Chironomus thummi with different genome sizes: homologous chromosome sites differ largely in their content of a specific H1 variant.
Mohr E, Trieschmann L, Grossbach U. Mohr E, et al. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9308-12. doi: 10.1073/pnas.86.23.9308. Proc Natl Acad Sci U S A. 1989. PMID: 2687879 Free PMC article. - Intrinsic Multienzyme-like Activities of the Nanoparticles of Mn and Fe Cyano-Bridged Assemblies.
Zhang Y, Kudriashov D, Pershina L, Offenhäusser A, Mourzina Y. Zhang Y, et al. Nanomaterials (Basel). 2022 Jun 17;12(12):2095. doi: 10.3390/nano12122095. Nanomaterials (Basel). 2022. PMID: 35745431 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Other Literature Sources
Research Materials
Miscellaneous