Abstract
An enzyme immunoassay kit for measurement of serum insulin was developed. This kit utilizes as its assay principle the sandwich method, using the insolubilized anti-insulin antibody and the enzyme-labeled anti-insulin antibody. The anti-insulin antibody was obtained by immunization of guinea pigs with porcine or bovine insulin. The enzyme-labeled anti-insulin antibody was obtained by binding horseradish peroxidase to the anti-insulin antibody by the periodic acid method. The insolubilized anti-insulin antibody was prepared by allowing the anti-insulin antibody to bind to plastic beads. The enzyme activity was measured as increased absorbance at 500 nm with 5-aminosalicylic acid and H 2O 2 as substrate. The measurement of the intensity of fluorescence with p-cresol and H 2O 2 as substrate also made the measurement of the enzyme activity in a short time (10 min) possible. The minimal detectable level of serum insulin with this kit was 5 μU/ml, with coefficients of variation in the range of 2.9–5.2% (for intra-assay) and 4.2–8.7% (for inter-assay). The measurements of serum insulin with this kit and those by radioimmunoassay were intimately correlated with each other (correlation coefficient, r = 0.996).
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