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Abstract
An electrochemical method to determine alanine aminotransferase (ALT) activity over
its normal and elevated physiological range was developed based upon detection of
L-glutamate at a glutamate oxidase-modified platinum electrode. Measurements were
carried out in the presence of ALT co-substrates L-alanine and alpha-ketoglutarate
and current response from either the oxidation of hydrogen peroxide or the re-oxidation
of the mediator ferrocene carboxylic acid was employed. The enzyme electrode was tested
over a 6-month period and found to retain 79% of its original activity towards ALT
detection with >200 measurements performed over this time. Signals associated with
interfering electroactive species (ascorbic acid and uric acid) were eliminated using
background subtraction at a denatured glutamate oxidase enzyme electrode. The sensitivity
of the device was found to be 0.845 nA U(-1) L ALT with t(90)=180 s, linear range
10-1000 U L(-1) and LOD of 3.29 U L(-1) using amperometry at E(app)=0.4 V vs. Ag/AgCl
at 308 K (35 degrees C).