Tyrosinase activity was assayed in black and white human foreskin samples by measuring both the hydroxylation of tyrosine to dopa (tyrosine hydroxylase activity) and the conversion of [14C]tyrosine to [14C]melanin (melanin synthesis assay). Enzyme activity was found both in the particulate (75%) and soluble (25%) fractions of the cell. Membrane-bound tyrosinase was readily solubilized by either zwitter-ionic or nonionic detergents. The anionic detergent, sodium cholate, inhibited enzyme activity. Tyrosinase activity in black foreskin homogenates averaged almost three times that in white skin samples (33.8 pmols 3H2O/h/mg skin in black and 12.71 pmoles 3H2O/h/mg skin in white skin), although considerable overlap in activities existed among the two groups. Tyrosinase activities measured with two separate assays, tyrosine hydroxylase and [14C]melanin assays, were similar, suggesting that tyrosine hydroxylase activity is tightly coupled to melanin synthesis. Tyrosinase activity determined by either assay method generally correlated with skin melanin content. Kinetic analysis of tyrosinase from black and white foreskin revealed a Km for tyrosine of 2.5 X 10(-4) M in both skin types. Immunotitration experiments suggested that the difference in tyrosinase activities between white and black skin may be due, not only to different amounts of enzyme present in the melanocytes, but also possibly to differences in the catalytic activities of the enzyme found in melanocytes of black and white skin.