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A sandwich-type immunoassay method for measurement of the as subunit of S100 protein in human biological fluids was developed by use of affinity-purified antibodies raised in rabbits with human S l00a0 (aa form ofS 100 protein) as immunogen. The assay system consisted of polystyrene balls with immobilized antibody F(ab')2 fragments and the same antibody Fab’ fragments labeled with ,8-D-galactosidase from Escherichia coli. The minimum detection limit of the assay was 3 pg S100a0 per assay tube. The assay cross-reacted about 20% with Sl00a (afi form of S100 protein), which contain an a subunit in the molecule, but showed no cross-reactivity with S l00b (BB form of S100 protein), indicating that the assay was specific to the a subunit of S100 protein (S100-0:). Coefficients of variation in within-run and between-run precision studies for serum and urine S100-0: were ~<15°/0. Concentrations of serum S100-a in healthy adults ranged from <0.060—0.464 nglml, and were significantly higher in male than in female. Concentrations in urine S100-or in normal adults ranged from 0.033 to 0.623 ng/ml showing no significant difference between the both sexes. Parotid saliva also contained a relatively high level (average value of 0.411 ng/ml) of S100-0:, which was probably derived from serous acini of parotid gland. A preliminary determination of S100-0: in urine samples from patients with kidney diseases showed that the S100-0: concentrations were enhanced in some patients with renal cell carcinoma, nephritis and nephrosis. S100 protein is an acidic and calciurn—binding protein primarily found in the bovine brain by Moore (l4). However, the biological function of S100 protein has been little elucidated. Isobe er al. (2-4) found that S100 protein is not a single component, but it is composed of at least three forms, Sl00a9, Sl00a and Sl00b, which are dimers with the subunit composition of aa, ab’ and 5,6, respectively. S100 protein had been considered to be located mostly in the brain as Sl00b and Sl00a (13). Recently, however, it has been found that S100 protein is also present in the -heart and skeletal muscles at high levels (9, 10) as the aa form (Sl00a0). Kidney also contains a considerable concentration of Sl00a0 mainly in the epithelial cells of proximal tubules, collecting tubules and Henle’s loops (7). Renal cell carcinoma, which is believed to be derived from the epithelial cell of proximal renal tubules (1), also produces a high level of Sl00a0, and serum Sl00a@ concentrations were elevated in some patients with renal cell carcinoma (7). For measuring Sl00a@ (or a subunit of S100 protein) in human sera or tissue extracts, we have been employing the immunoassay

<b>ENZYME IMMUNOASSAY FOR MEASUREMENT OF THE α SUBUNIT OF S100 PROTEIN IN HUMAN BIOLOGICAL </b><b>FLUIDS </b>