In peroxidase

Kupriyanova E.V. Ezhova T.A. Lebedeva O.V. Shestakov S.V. (2006) Intraspecific polymorphism in peroxidases genes located on Arabidopsis thaliana chromosome 5 // Biological Bull. N. 4. P. 437-447. 

Siegel S.M. (1957) Non-enzymic macromolecules as matrices in biological synthesis. The role of polysaccharides in peroxidase catalyzed lignin polymer formation from eugenol // J. Amer. Chem. Soc. V. 79. P. 1628-1632... 

Holtzman, E., Freeman, A. R. and Kashner, A. Stimulation-dependent alterations in peroxidase uptake at lobster neuromuscular junctions. Science 173 733-736,1971. 

As shown in Table 12,H202 and fBuOOH have been used frequently as oxygen donors in peroxidase-catalyzed sulfoxidations. Other achiral oxidants, e.g. iodo-sobenzene and peracids, are not accepted by enzymes and, therefore, only racemic sulfoxides were found (c.f. entries 34-36). Interestingly, racemic hydroperoxides oxidize sulfides to sulfoxides enantioselectively under CPO catalysis [68]. In this reaction, not only the sulfoxides but also the hydroperoxide and the corresponding alcohol were produced in optically active form by enzyme-catalyzed kinetic resolution (cf. Eq. 3 and Table 3 in Sect. 3.1). 

Most researchers have felt that biochemical changes in plant tissues are associated with so many normal growth and stress phenomena that they would have no relevance in field evaluations of air pollution effects. Keller has associated changes in peroxidase activity with different pollution stresses (fluoride and oxidants) in apricot and white ash growing in areas of high pollution, as opposed to those of low pollution. This study suffers from lack of pollution monitoring (although leaves were... 

Curtis, C. R., and R. K. Howell. Increases in peroxidase isoenzyme activity in bean leaves exposed to low doses of ozone. Phytopathology 61 1306-1307, 1971. 

As in peroxidases, globins, and P450s, HO-1 has a helix over the distal surface of the heme (Figs. 16,18). In other heme proteins side chains from the distal helix provide the primary contacts with the heme as well as side chains that interact with heme ligands. In sharp contrast, the distal helix in HO-1 lies much closer to the heme such that backbone atoms form the primary heme contacts. In addition, there is no neighboring residue that could serve the same fimction as the distal His in the globins and peroxidases for interaction with iron-linked ligands. 

Peroxidase activity in flight seedlings was reduced to essentially the same extent as PAL activity. Again, the average difference in the STS-3 (—19.0%) and STS-51F (—20.2%) experiments were similar (Table V). As with PAL activity the reduction in peroxidase activity in flight seedlings was similar along the pine hypocotyl. 

In a recent study (54), we showed increased activities of two enzymes of the general phenylpropanoid pathway, PAL and 4-coumarate CoA lig-ase, as well as one enzyme of the specific pathway of lignin biosynthesis, cinnamy 1-alcohol dehydrogenase (CAD), in resistant plants at the time of the hypersensitive host cell death. On the other hand, decreased activities were observed at the same time with susceptible host plants (54). Furthermore, we showed that the well known increase in peroxidase activities, which is strong in resistant and only weak in susceptible plants (55-58), is at least partly due to the increased activity of the lignin biosynthetic pathway (54,59). 

Hirota, S., Nishioka, T., Shimoda, T., Miura, K, Ansal, T., and Takahama, U., Quercetin gluco-sides are hydrolysed to quercetin in human oral cavity to participate in peroxidase-dependent scavenging of hydrogen peroxide. Food Set Technol Res., 7, 239, 2001. 

Wash and incubate the blots in peroxidase-labeled antispecies antibody at room temperature, as indicated m Table 1. 

Thorpe, J. R., and Hall, J. L., 1984, Chronology and elicitation of changes in peroxidase and phenylalanine ammonia-lyase activities in wounded wheat leaves in response to inoculation with Botrytis cinerea, Physiol. Plant Pathol. 25 363-379. 

The sections are incubated in a primary antibody (diluted appropriately) for 72 hr at 4°C in a sealed humid chamber the incubation is carried out by applying droplets of the antibody to the sections. After being rinsed in the buffer, the sections are incubated for 90min in secondary antiserum diluted 1 50 with PBX (0.3% Triton X-100, 0.01% sodium azide and 0.1 M phosphate buffer) and then treated for 1 hr under agitation in peroxidase-antiperoxidase (PAP), diluted 1 100 with PBX, in a sealed humid chamber in both cases. 

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