scholarly journals Cross-linking of Horseradish Peroxidase Enzyme to Fine Particles Generated by Nano Spray Dryer B-90

2015 ◽  
Vol 59 (3) ◽  
pp. 209-214 ◽  
Author(s):  
Laura Amina Dahili ◽  
Tivadar Feczkó
Keyword(s):  
Horseradish Peroxidase ◽  
Fine Particles ◽  
Cross Linking ◽  
Spray Dryer ◽  
Peroxidase Enzyme

scholarly journals A comparative study of horseradish peroxidase conjugates prepared with a one-step and a two-step method.

1975 ◽  
Vol 23 (3) ◽  
pp. 200-207 ◽  
Author(s):  
D M Boorsma ◽  
G L Kalsbeek
Keyword(s):  
Horseradish Peroxidase ◽  
Lupus Erythematosus ◽  
Cross Linking ◽  
Discoid Lupus Erythematosus ◽  
Gel Chromatography ◽  
Ammonium Sulfate Precipitation ◽  
Step Method ◽  
One Step ◽  
Cryostat Sections ◽  
Unfixed Cryostat

In this study we compared horseradish peroxidase (HRP)-labeled rabbit antihuman immunoglobulin G (IgG) conjugates, prepared by a one-step and a two-step method. Glutaraldehyde was used as a cross-linking agent. Two methods were used for removing unconjugated HRP: Sephadex G-200 gel chromatography and ammonium sulfate precipitation. The conjugates were characterized immunologically, immunochemically and enzymatically. The immunohistoenzymic properties of the conjugates were tested on unfixed cryostat sections of the skin of patients with chronic discoid lupus erythematosus. The influence of the presence of unconjugated HRP and unconjugated IgG was studied. Optimal results were obtained with conjugates prepared by a two-step method. Removing unconjugated HRPimproved the immunohistoenzymic properties of the conjugates. Conjugated and unconjugated IgG could be separated by Sephadex G-200 gel chromatography.

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.

Controlled formation of protein nanoparticles by enzymatic cross-linking of α-lactalbumin with horseradish peroxidase

2014 ◽  
Vol 36 ◽  
pp. 53-59 ◽  
Author(s):  
Surender K. Dhayal ◽  
Harry Gruppen ◽  
Renko de Vries ◽  
Peter A. Wierenga
Keyword(s):  
Horseradish Peroxidase ◽  
Cross Linking ◽  
Protein Nanoparticles

Application of zero-length cross-linking to form lysozyme, horseradish peroxidase and lysozyme–peroxidase dimers: Activity and stability

2007 ◽  
Vol 41 (5) ◽  
pp. 624-630 ◽  
Author(s):  
Hashem Yaghoubi ◽  
Khosro Khajeh ◽  
Saman Hosseinkhani ◽  
Bijan Ranjbar ◽  
Hossein Naderi-Manesh
Keyword(s):  
Horseradish Peroxidase ◽  
Cross Linking

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

The role of Arginine 38 in horseradish peroxidase enzyme revisited: A computational investigation

2009 ◽  
Vol 141 (1) ◽  
pp. 87-93 ◽  
Author(s):  
Simone Tatoli ◽  
Costantino Zazza ◽  
Nico Sanna ◽  
Amedeo Palma ◽  
Massimiliano Aschi
Keyword(s):  
Horseradish Peroxidase ◽  
Computational Investigation ◽  
Peroxidase Enzyme
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