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Development of an electrochemical-based aspartate aminotransferase nanoparticle ir-C biosensor for screening of liver diseases.

Hsueh CJ, Wang JH, Dai L, Liu CC - Biosensors (Basel) (2012)

Bottom Line: Aspartate aminotransaminase (AST) is a hepatocelluar enzyme released into the bloodstream when hepatic cells are damaged, resulting in elevated blood levels of AST.This biosensor is capable of measuring AST levels in a phosphate buffer and undiluted human serum over the concentration range of 0 to 0.89 μg/mL AST concentration (corresponding to 0-250 UL-1 specific activity).The biosensor operates at relatively low oxidation potential (+0.3 volt (V) versus the printed Ag/AgCl), minimizing any potential chemical interference in human serum.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemical Engineering and Electronics Design Center, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106, USA. cxh300@case.edu.

ABSTRACT
Aspartate aminotransaminase (AST) is a hepatocelluar enzyme released into the bloodstream when hepatic cells are damaged, resulting in elevated blood levels of AST. A single use, disposable biosensor prototype, composed of catalytic iridium nano-particles dispersed on carbon paste, was developed to detect enzymatically-produced H2O2 in AST-mediated reactions. This biosensor is capable of measuring AST levels in a phosphate buffer and undiluted human serum over the concentration range of 0 to 0.89 μg/mL AST concentration (corresponding to 0-250 UL-1 specific activity). The biosensor operates at relatively low oxidation potential (+0.3 volt (V) versus the printed Ag/AgCl), minimizing any potential chemical interference in human serum. The measurements of AST in human serum using the biosensor compared well with those measured by standard hospital spectrophotometric assays. This Ir-C biosensor may be useful for AST measurements in the clinical environment.

No MeSH data available.


Reaction mechanism on electrochemical assays of AST by measuring enzymatically generated H2O2 from the interaction between L-glutamate and glutamate oxidase.
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biosensors-02-00234-f009: Reaction mechanism on electrochemical assays of AST by measuring enzymatically generated H2O2 from the interaction between L-glutamate and glutamate oxidase.


Development of an electrochemical-based aspartate aminotransferase nanoparticle ir-C biosensor for screening of liver diseases.

Hsueh CJ, Wang JH, Dai L, Liu CC - Biosensors (Basel) (2012)

Reaction mechanism on electrochemical assays of AST by measuring enzymatically generated H2O2 from the interaction between L-glutamate and glutamate oxidase.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4263573&req=5

biosensors-02-00234-f009: Reaction mechanism on electrochemical assays of AST by measuring enzymatically generated H2O2 from the interaction between L-glutamate and glutamate oxidase.
Bottom Line: Aspartate aminotransaminase (AST) is a hepatocelluar enzyme released into the bloodstream when hepatic cells are damaged, resulting in elevated blood levels of AST.This biosensor is capable of measuring AST levels in a phosphate buffer and undiluted human serum over the concentration range of 0 to 0.89 μg/mL AST concentration (corresponding to 0-250 UL-1 specific activity).The biosensor operates at relatively low oxidation potential (+0.3 volt (V) versus the printed Ag/AgCl), minimizing any potential chemical interference in human serum.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemical Engineering and Electronics Design Center, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106, USA. cxh300@case.edu.

ABSTRACT
Aspartate aminotransaminase (AST) is a hepatocelluar enzyme released into the bloodstream when hepatic cells are damaged, resulting in elevated blood levels of AST. A single use, disposable biosensor prototype, composed of catalytic iridium nano-particles dispersed on carbon paste, was developed to detect enzymatically-produced H2O2 in AST-mediated reactions. This biosensor is capable of measuring AST levels in a phosphate buffer and undiluted human serum over the concentration range of 0 to 0.89 μg/mL AST concentration (corresponding to 0-250 UL-1 specific activity). The biosensor operates at relatively low oxidation potential (+0.3 volt (V) versus the printed Ag/AgCl), minimizing any potential chemical interference in human serum. The measurements of AST in human serum using the biosensor compared well with those measured by standard hospital spectrophotometric assays. This Ir-C biosensor may be useful for AST measurements in the clinical environment.

No MeSH data available.