A novel method for synthesis of water-soluble polypyrrole with horseradish peroxidase enzyme

2004 ◽  
Vol 94 (1) ◽  
pp. 254-258 ◽  
Author(s):  
Mohammad Reza Nabid ◽  
Ali Akbar Entezami
Keyword(s):  
Horseradish Peroxidase ◽  
Water Soluble ◽  
Peroxidase Enzyme ◽  
Novel Method

scholarly journals Inhibitory effect of retinol acetate on horseradish peroxidase

2013 ◽  
Vol 67 (3) ◽  
pp. 419-426
Author(s):  
Vladan Djuric ◽  
Nebojsa Deletic ◽  
Vesna Stankov-Jovanovic ◽  
Ranko Simonovic
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Enzymatic Reaction ◽  
Inhibitory Effect ◽  
Enzyme Concentration ◽  
Water Soluble ◽  
Primary Role ◽  
Retinol Acetate ◽  
Peroxidase Enzyme

Primary role of peroxidase enzyme is to decompose endogenous hydrogen peroxide, when oxygen radical is being replaced by a less potent radical, which is its cosubstrates oxidized form. During this study, catalytic activity of horseradish peroxidase has been observed in the presence of antioxidants from vitamin group, such as C, E and A, i.e. their water-soluble forms. It was found that vitamin E showed no effect on the enzyme activity and fate of cosubstrate radicals from the group of benzidine derivatives. Vitamin C proceeds enzymatic reaction showing its antioxidative character, and absorbs electrons from radicals, bringing cosubstrate back to its relaxed state. On the other hand, vitamin A plays a role of uncompetitive peroxidase inhibitor, which is visible through decreasing initial rate of catalytic reaction, and is reflected as virtual decrease of enzyme concentration. Furthermore, it prolongs life of endogenous hydrogen peroxide, which could potentially lead to oxidative stress of cells. This inhibitory effect can be used in analytical purpose, for determination of retinol acetate content in a sample.

Separation and purification of horseradish peroxidase from horseradish roots using a novel integrated method

2021 ◽  
Author(s):  
Wei Ji ◽  
Wenmei Ao ◽  
Mengqiu Sun ◽  
Chunlai Feng ◽  
Yun Wang
Keyword(s):  
Horseradish Peroxidase ◽  
Phase Extraction ◽  
Separation And Purification ◽  
Two Phase ◽  
Affinity Precipitation ◽  
Integrated Method ◽  
Novel Method ◽  
Temperature Controlled ◽  
Aqueous Two Phase Extraction

The aim of the present work was to develop a novel method integrating two-step aqueous two-phase extraction and temperature-controlled affinity precipitation for the separation and purification horseradish peroxidase (HRP) from...

Micropatterned array to assess the interaction of single platelets with platelet factor 4-heparin-IgG complexes

2014 ◽  
Vol 111 (05) ◽  
pp. 862-872 ◽  
Author(s):  
Krystin Krauel ◽  
Nikolay Medvedev ◽  
Raghavendra Palankar ◽  
Andreas Greinacher ◽  
Mihaela Delcea
Keyword(s):  
Calcium Imaging ◽  
Cell Function ◽  
Platelet Factor 4 ◽  
Water Soluble ◽  
Cell Level ◽  
Platelet Factor ◽  
Ligand Density ◽  
Heparin Complexes ◽  
Novel Method ◽  
Platelet Aggregates

SummaryWe report a strategy to generate by electron beam lithography high fidelity micropatterned arrays to assess the interaction of single platelets with immobilised ligands. As a proof-of-principle we functionalised the microarrays with platelet factor 4 (PF4)-heparin-IgG complexes. We embedded biotinylated water-soluble quantum dots into polyethylene glycol (PEG)-coated micropatterned arrays and functionalised them via streptavidin to bind biotinylated ligands, here biotinylated-PF4/heparin complexes. The integrity of the PF4/heparin-complexes was shown by binding of anti-PF4/heparin antibodies. Ligand density was quantified by immunofluorescence and immunogold antibody labelling. Real-time calcium imaging was employed for read-out of single platelets activated on micropatterned surfaces functionalised with PF4/heparin-IgG complexes. With the smallest micropatterns (0.5x0.5 µm) we show that single platelets become strongly activated by binding to surface-immobilised PF4/heparin-IgG, while on larger micropatterns (10x10 µm), platelet aggregates formed. These findings that HIT antibodies can cause platelet activation on microarrays illustrate how this novel method opens new avenues to study platelet function at single cell level. Generating functionalized microarray surfaces to which highly complex ligands can be bound and quantified has the potential for platelet and other cell function assays integrated into high-throughput microfluidic microdevices.

Studies on the dehydrogenative polymerizations of monolignol β-glycosides. Part 2: Horseradish peroxidase-catalyzed dehydrogenative polymerization of isoconiferin

Holzforschung ◽  
2006 ◽  
Vol 60 (5) ◽  
pp. 513-518 ◽  
Author(s):  
Yuki Tobimatsu ◽  
Toshiyuki Takano ◽  
Hiroshi Kamitakahara ◽  
Fumiaki Nakatsubo
Keyword(s):  
Horseradish Peroxidase ◽  
Water Solubility ◽  
Homogeneous System ◽  
Degree Of Polymerization ◽  
Coniferyl Alcohol ◽  
Water Soluble ◽  
Optimum Conditions ◽  
Spectroscopic Analyses ◽  
Dehydrogenation Polymer ◽  
Dehydrogenative Polymerization

Abstract Dehydrogenative polymerization of isoconiferin (IC; coniferyl alcohol γ-O-β-D-glucopyranoside) catalyzed by horseradish peroxidase (HRP) was carried out. The polymerization of IC proceeded in a homogeneous system, resulting in a water-soluble dehydrogenation polymer (IC-DHP). The degree of polymerization (DP) of IC-DHP was significantly higher than that of a standard dehydrogenative polymer (CA-DHP) obtained from coniferyl alcohol (CA) in a heterogeneous system. Under optimum conditions, the DP of IC-DHP was 44 (M n=1.5×104), whereas that for CA-DHP was only 11 (M n=3.0×103, as acetate). Spectroscopic analyses confirmed that IC-DHP has a lignin-like structure containing D-glucose moieties attached to the lignin side-chains. The D-glucose unit introduced into γ-O position of CA essentially influenced the water solubility and molecular mass of the resulting DHP.

Highly sensitive biosensing of phenol based on the adsorption of the phenol enzymatic oxidation product on the surface of an electrochemically reduced graphene oxide-modified electrode

2018 ◽  
Vol 10 (23) ◽  
pp. 2731-2739 ◽  
Author(s):  
Amir Kaffash ◽  
Hamid R. Zare ◽  
Khosrow Rostami
Keyword(s):  
Graphene Oxide ◽  
Horseradish Peroxidase ◽  
Reduced Graphene Oxide ◽  
Modified Electrode ◽  
Enzymatic Oxidation ◽  
Reduced Graphene ◽  
Highly Sensitive ◽  
Electrochemically Reduced Graphene Oxide ◽  
Phenol Determination ◽  
Peroxidase Enzyme

An electrochemically reduced graphene oxide and horseradish peroxidase enzyme modified electrode has been used for phenol determination.

Electrochemical AFM investigation of horseradish peroxidase enzyme electro-immobilization with polypyrrole conducting polymer

2009 ◽  
Vol 159 (5-6) ◽  
pp. 541-545 ◽  
Author(s):  
Mohammed ElKaoutit ◽  
Ahmed Hosny Naggar ◽  
Ignacio Naranjo-Rodriguez ◽  
Manuel Dominguez ◽  
José Luis Hidalgo-Hidalgo de Cisneros
Keyword(s):  
Horseradish Peroxidase ◽  
Conducting Polymer ◽  
Peroxidase Enzyme

Role of 2,4-Dichlorophenol in the Oxidation of Estradiol by Uterine and Horseradish Peroxidase

1973 ◽  
Vol 51 (7) ◽  
pp. 1066-1071 ◽  
Author(s):  
C. R. Lyttle ◽  
T. McNabb ◽  
P. H. Jellinck
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Water Soluble

The role of 2,4-dichlorophenol in enhancing the conversion of [4-14C]estradiol to water-soluble products by a uterine preparation in the presence of hydrogen peroxide has been investigated. The addition of this phenol to a solution of uterine or horseradish peroxidase in 8 M urea restored the activity of the enzyme and also that of horseradish peroxidase inactivated by heating. It also protected the enzyme from inactivation during incubation. It is proposed that 2,4-dichlorophenol exerts its effect by activating peroxidase and protecting the enzyme from inactivation by the products of the reaction.

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