Phenol sulfotransferase (PST) catalyzes the sulfate conjugation of catecholamines and of phenolic drugs. Human platelet PST exists in at least a thermolabile form (TL PST) and a thermostable form (TS PST). The mean basal level of platelet TS PST activity in samples from American blacks is significantly higher than the basal activity in samples from whites. We carried out the studies reported here to determine whether the higher basal TS PST activity in platelet homogenates from blacks was biochemically similar to the lower basal activity in samples from whites. We also characterized variations in TS PST thermal stability. Platelet TS PST activities in samples from the two groups were almost identical with respect to pH optima, Michaelis-Menten constant values for substrates, and susceptibilities to inhibition by 2,6-dichloro-4-nitrophenol and sodium chloride. Thermolabile and thermostable TS PST were present in samples from both blacks and whites. Thermal stabilities of TS PST in samples from 167 volunteers (104 blacks, 63 whites) were expressed as heated sample-to-control sample ratios. Bimodal frequency distribution histograms of the heated-to-control ratios revealed subgroups of samples with thermolabile TS PST activities from 13.5% of blacks (heated-to-control ratio less than 0.32) and 12.7% of whites (heated-to-control ratio less than 0.27). The mean heated-to-control ratio for thermostable TS PST from blacks was significantly higher than that from whites (0.52 +/- 0.01 vs 0.43 +/- 0.01, respectively, mean +/- SEM; p less than 0.0001). Our studies demonstrated the similarity of biochemical properties of platelet TS PST at the extremes of basal activity. They also showed equivalent subgroups of blacks and whites with thermolabile TS PST. The results are an important initial step toward testing the hypothesis that inheritance may be one factor in the regulation of basal levels of activities and thermal stabilities of platelet TS PST from American blacks.