Abstract
The initial step in human erythrocyte lysis by oleate at pH 7.2 + 0.1 and concentrations below 8 x 10-4 [image] involves erythrocyte-oleate binding; oleate binding by a standard number of erythrocytes in a fixed volume is a function of oleate concentration, temperature, and contact time. Once lytic quantities of oleate are bound, hemolysis proceeds at pH 7.2 [plus or minus] 0.1 as a function of quantity bound and of temperature. Lysis cannot be checked by repeated iced saline washings. A mean minimum of approximately 7 x 10-9 [mu]g of sodium oleate is required per erythrocyte at 37[degree]C, pH 7.1 for lysis at rates detectably faster than controls; the sodium oleate binding mechanism appears saturated with a mean of approximately 111 x 10-9 [mu]g/erythrocyte. Lowering of solution surface tension by oleate did not influence hemolysis rates. Cyanide was found to retard oleate hemolysis but other non-specific enzyme inhibitors failed to do so. Following oleate hemolysis, hemolytic substances were released which probably represented oleate or products of oleate-erythrocyte interaction.

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