Effect of antibodies to glucose oxidase in the apoenzyme reactivation immunoassay system.
The use of antiserum to glucose oxidase in the apoenzyme reactivation immunoassay system (ARIS) is described. Formation of an immune complex between apoglucose oxidase and antibodies to native glucose oxidase enables FAD conjugates to be detected with greater sensitivity and at higher temperatures. In the absence of antiserum to glucose oxidase, optimum activity with theophylline-FAD was at 23 degrees C whereas in the presence of the antiserum the optimum shifted to 32 degrees C and was accompanied by a sixfold increase in activity. At 37 degrees C in the absence of antiserum very little activity is found. The use of the antiserum makes it possible to perform ARIS assays at 37 degrees C and this is illustrated by description of an assay for theophylline.
D000906:Antibodies; D000936:Antigen-Antibody Complex; D001051:Apoenzymes / Q000378:metabolism*; D001059:Apoproteins / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000032:analysis; D005949:Glucose Oxidase / Q000378:metabolism*; D007106:Immune Sera; D007118:Immunoassay; D007700:Kinetics; D013053:Spectrophotometry / Q000379:methods
D000906:Antibodies; D000936:Antigen-Antibody Complex; D001051:Apoenzymes; D001059:Apoproteins; D007106:Immune Sera; D005182:Flavin-Adenine Dinucleotide; D005949:Glucose Oxidase