An amperometric hemoglobin A1c biosensor based on immobilization of fructosyl amino acid oxidase onto zinc oxide nanoparticles–polypyrrole film

2012 ◽  
Vol 430 (2) ◽  
pp. 156-162 ◽  
Author(s):  
Sheetal Chawla ◽  
Chandra Shekhar Pundir
Keyword(s):  
Zinc Oxide ◽  
Amino Acid ◽  
Zinc Oxide Nanoparticles ◽  
Hemoglobin A1c ◽  
Oxide Nanoparticles ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Polypyrrole Film ◽  
Fructosyl Amino Acid Oxidase

scholarly journals Review of Fructosyl Amino Acid Oxidase Engineering Research: A Glimpse into the Future of Hemoglobin A1c Biosensing

2009 ◽  
Vol 3 (3) ◽  
pp. 585-592 ◽  
Author(s):  
Stefano Ferri ◽  
Seungsu Kim ◽  
Wakako Tsugawa ◽  
Koji Sode
Keyword(s):  
Amino Acid ◽  
Hemoglobin A1c ◽  
Point Of Care ◽  
Detection Methods ◽  
Future Research ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Engineering Research ◽  
Glycated Proteins ◽  
Fructosyl Amino Acid Oxidase

Glycated proteins, particularly glycated hemoglobin A1c, are important markers for assessing the effectiveness of diabetes treatment. Convenient and reproducible assay systems based on the enzyme fructosyl amino acid oxidase (FAOD) have become attractive alternatives to conventional detection methods. We review the available FAOD-based assays for measurement of glycated proteins as well as the recent advances and future direction of FAOD research. Future research is expected to lead to the next generation of convenient, simple, and economical sensors for glycated protein, ideally suited for point-of-care treatment and self-monitoring applications.

scholarly journals New Enzymatic Assay for Glycohemoglobin

2003 ◽  
Vol 49 (2) ◽  
pp. 269-274 ◽  
Author(s):  
Ikunosuke Sakurabayashi ◽  
Tatsurou Watano ◽  
Satoshi Yonehara ◽  
Kaori Ishimaru ◽  
Kaoru Hirai ◽  
...  
Keyword(s):  
Amino Acid ◽  
Blood Cells ◽  
Hplc Method ◽  
Enzymatic Assay ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Blood Samples ◽  
Total Hemoglobin ◽  
Patients With Diabetes ◽  
Fructosyl Amino Acid Oxidase

Abstract Background: Previous methods to measure glycohemoglobin (GHb) have been time-consuming or imprecise; we therefore developed a new enzymatic assay for GHb. Methods: Blood cells were first hemolyzed, and hemoglobin was digested with protease to yield fructosyl amino acid. Fructosyl amino acid oxidase acts on the fructosyl amino acid and generates hydrogen peroxide, which reacts with chromogens in the presence of peroxidase. Total hemoglobin was measured spectrometrically in the same reaction tube. The results were reported as the ratio of the concentrations of GHb and hemoglobin. Results: The measured values were comparable to those determined with a HPLC method and with an immunoassay in blood samples from 2854 patients with diabetes. Regression analysis for the enzymatic assay (y) vs the HPLC method (x) produced the following: r = 0.979; slope, 0.994 [95% confidence interval (CI), 0.986–1.001]; y-intercept, 0.04% (95% CI, −0.09% to 0.01%); n = 2854. For the enzymatic assay (y) vs the immunoassay (x), the regression statistics were as follows: r = 0.982; slope, 1.002 (95% CI, 0.995–1.009); y-intercept, 0% (95% CI, −0.05% to 0.05%); n = 2854. Conclusions: The values measured by the new enzymatic assay are sufficiently correlated with those of the conventional HPLC method and immunoassay, but the proposed assay for GHb is rapid and has high precision.

Alteration of substrate specificity of fructosyl-amino acid oxidase from Fusarium oxysporum

2007 ◽  
Vol 74 (4) ◽  
pp. 813-819 ◽  
Author(s):  
Maki Fujiwara ◽  
Jun-ichi Sumitani ◽  
Shinji Koga ◽  
Issei Yoshioka ◽  
Takuji Kouzuma ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Fusarium Oxysporum ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Fructosyl Amino Acid Oxidase

scholarly journals Distribution and properties of fructosyl amino acid oxidase in fungi.

1995 ◽  
Vol 61 (12) ◽  
pp. 4487-4489 ◽  
Author(s):  
N Yoshida ◽  
Y Sakai ◽  
M Serata ◽  
Y Tani ◽  
N Kato
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Fructosyl Amino Acid Oxidase

scholarly journals Unexpected insights into antibacterial activity of zinc oxide nanoparticles against methicillin resistantStaphylococcus aureus(MRSA)

Nanoscale ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 4927-4939 ◽  
Author(s):  
Usha Kadiyala ◽  
Emine Sumeyra Turali-Emre ◽  
Joong Hwan Bahng ◽  
Nicholas A. Kotov ◽  
J. Scott VanEpps
Keyword(s):  
Zinc Oxide ◽  
Antibacterial Activity ◽  
Amino Acid ◽  
Mechanism Of Action ◽  
Zinc Oxide Nanoparticles ◽  
Sugar Metabolism ◽  
Acid Synthesis ◽  
Pyrimidine Biosynthesis ◽  
Oxide Nanoparticles ◽  
Amino Acid Synthesis

Zinc oxide nanoparticles cause marked up-regulation of pyrimidine biosynthesis and sugar metabolism but consistent down-regulation of amino acid synthesis in MRSA, suggesting a previously unrecognized mechanism of action.

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