Hemolysis of mouse erythrocytes by ferriprotoporphyrin IX and chloroquine. Chemotherapeutic implications.
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منابع مشابه
Hemolysis of mouse erythrocytes by ferriprotoporphyrin IX and chloroquine. Chemotherapeutic implications.
Incubation of a 0.5% suspension of washed normal mouse erythrocytes with ferriprotoporphyrin IX (FP) for 2.5 h at 37 degrees C and pH 7.4 results in sufficient membrane damage to produce hemolysis. A sigmoidal dose-response curve is followed with 50% hemolysis being produced by 4 microM FP. Complete hemolysis is produced by 6 microM FP. The hemolytic process has at least two phases: a lag phase...
متن کاملMechanism of hemolysis induced by ferriprotoporphyrin IX.
Incubation of a 0.5% suspension of washed, normal mouse erythrocytes with ferriprotoporphyrin IX (FP) at 37 degrees C and pH 7.4 caused potassium loss, swelling, increased susceptibility to hypotonic lysis, and finally hemolysis. Hemolysis was not inhibited by incubation in the dark, malonyldialdehyde was not produced, and various free radical scavengers had no effect on the hemolysis. Only the...
متن کاملIntracellular Ferriprotoporphyrin IX Is
Human erythrocytes were treated with menadione to oxidatively denature hemoglobin and release ferriprotoporphyrin IX (ferriheme, FP) intracellularly. The high affinity of FP for chloroquine was used to detect its release. After incubation for 1 hr at 37’C and pH 7.4 with 0.5 mM menadione, erythrocytes bound 14C-chloroquine with an apparent dissociation constant of 1O M. Untreated erythrocytes d...
متن کاملIntracellular ferriprotoporphyrin IX is a lytic agent.
Human erythrocytes were treated with menadione to oxidatively denature hemoglobin and release ferriprotoporphyrin IX (ferriheme, FP) intracellularly. The high affinity of FP for chloroquine was used to detect its release. After incubation for 1 hr at 37 degrees C and pH 7.4 with 0.5 mM menadione, erythrocytes bound 14C-chloroquine with an apparent dissociation constant of 10(-6)M. Untreated ery...
متن کاملCellular Uptake of Chloroquine Is Dependent on Binding to Ferriprotoporphyrin IX and Is Independent of NHE Activity in Plasmodium falciparum
Here we provide definitive evidence that chloroquine (CQ) uptake in Plasmodium falciparum is determined by binding to ferriprotoporphyrin IX (FPIX). Specific proteinase inhibitors that block the degradation of hemoglobin and stop the generation of FPIX also inhibit CQ uptake. Food vacuole enzymes can generate cell-free binding, using human hemoglobin as a substrate. This binding accounts for CQ...
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ژورنال
عنوان ژورنال: Journal of Clinical Investigation
سال: 1980
ISSN: 0021-9738
DOI: 10.1172/jci109925