Occurrence of Fructosyl-Amino Acid Oxidase-Reactive Compounds in Fungal Cells

2005 ◽  
Vol 69 (1) ◽  
pp. 258-260 ◽  
Author(s):  
Nobuyuki YOSHIDA ◽  
Kenji TAKATSUKA ◽  
Tohoru KATSURAGI ◽  
Yoshiki TANI
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Fructosyl Amino Acid Oxidase

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.

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.

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
Sign in / Sign up

Export Citation Format

Share Document