Abstract
Summary
1. The initial step in human erythrocyte lysis by oleate at pH 7.2 ± 0.1 and concentrations below 8 × 10-4 M 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. 2. Once lytic quantities of oleate are bound, hemolysis proceeds at pH 7.2 ± 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 × 10-9 μg of sodium oleate is required/erythrocyte at 37°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 × 10-9 μg/erythrocyte. 3. Lowered surface tension of oleate solutions does not influence hemolysis rates under conditions tested. 4. Cyanide retards oleate hemolysis; other non-specific enzyme inhibitors fail to do so. 5. Following oleate hemolysis, hemolytic substances are released; these probably represent oleate or products of oleate-erythrocyte interaction. It is suggested that oleate possesses the potential of inducing a decelerating hemolytic chain reaction.
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