beta-Glucosidase activity from normal human cultured fibroblasts was not affected by the presence of up to 0.1% (w/v) (1.86 mM) purified sodium taurocholate. At concentrations greater than 0.1%, there was a gradual decrease in activity. Conversely, beta-glucosidase activity from fibroblasts of three patients with juvenile onset Gaucher's disease was preferentially inhibited by the detergent at concentrations as low as 0.025% (0.46 mM). A 40% decrease in activity was observed at 0.1%. Crude sodium taurocholate was more potent in inhibiting beta-glucosidase activity from both the normal and Gaucher fibroblasts. However, very high background fluorescence and inconsistent results were observed when different batches of the crude taurocholate from the same or different sources were used. Similarly, beta-glucosidase activity from Gaucher splenic tissue homogenates, supernatant fluids (40,000 x g) and residue pellets was preferentially inhibited by purified sodium taurocholate. These findings indicate that the reliability and sensitivity of the enzyme assay for Gaucher's disease can be enhanced by determining beta-glucosidase activity in both the absence and presence of purified sodium taurocholate, particularly when variant cases with relatively high residual enzyme activity are encountered. In contrast to the enzyme from fibroblasts and spleens, beta-glucosidase activity from human placenta was markedly activated (greater than 300%) by the presence of 0.08% (1.49 mM) purified sodium taurocholate or 0.1 mM phosphatidyl serine, suggesting the presence of a predominate form of beta-glucosidase, possibly glucocerebroside beta-glucosidase, which is activated by the detergent. The apparent Michaelis constant (Km) for both the soluble and membrane-bound enzyme from normal fibroblasts was 1.6 +/- 0.1 mM. Kms from a patient with severe juvenile Gaucher's disease and two other patients with milder manifestations were 0.8 +/- 0.2 and 3.3 +/- 0.3 mM, respectively.