Effect of sulphydryl inhibition on the uptake of transferrin-bound iron by reticulocytes.
Iron transferrin, the highly stable carrier of plasma iron, may be dissociated, under physiological conditions, by sodium thioglycollate, a reaction which involves the formation of iron thioglycollate complexes. This suggested that sulphydryl radicals, which are the active groups in thioglycollate and related compounds, may play a part in the uptake of iron by immature red cells from iron transferrin. If this were so, it could be predicted that the sulphydryl inhibitor, p-hydroxymercuribenzoate, would depress the uptake of iron by reticulocytes. It is demonstrated here that inhibition of uptake of transferrin-bound iron by reticulocytes, which have been exposed to micromolar concentration of p-hydroxymercuribenzoate, is virtually complete. It is suggested that sulphydryl-containing compounds are intimately involved in the process of iron uptake by immature red cells.
D006801:Humans; D066298:In Vitro Techniques; D007501:Iron / Q000037:antagonists & inhibitors* / Q000378:metabolism; D007503:Iron Isotopes; D008628:Mercury / Q000494:pharmacology; D009942:Organometallic Compounds / Q000494:pharmacology; D012156:Reticulocytes / Q000187:drug effects / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000494:pharmacology* / Q000502:physiology; D014168:Transferrin / Q000378:metabolism*
D007503:Iron Isotopes; D009942:Organometallic Compounds; D013438:Sulfhydryl Compounds; D014168:Transferrin; D007501:Iron; D008628:Mercury