The erythrocyte transport and transfer of methylmercury to the tissues of the rainbow trout (Salmo gairdneri).

Methylmercury (MeHg) was found to be taken up rapidly and almost completely by trout red blood cells (RBC) both in vitro and in vivo. The binding of MeHg within the RBC was freely reversible both in vitro, as shown by the efflux of MeHg from RBCs suspended in protein solutions, and in vivo following intracardial (i.c.) injection of RBC-bound MeHg. Hemoglobin (Hb) appeared to be the main MeHg transport protein in trout blood since it bound 90% of whole blood Hg following an intragastric dose of Me203HgCl. MeHg, injected i.c. as MeHgS-cysteine, was found to be present in blood bound almost completely to hemoglobin 10 days post-injection. This suggests an ability of hemoglobin to compete for and bind MeHg bound to other sulfhydryl (-SH) compounds. The number of reactive -SH groups per molecule of trout Hb was determined to be 4 by amperometric titration with MeHgCl. The concentration of Hb reactive -SH groups in the trout RBC was calculated to be at least 20 mM. This accounts for the high affinity of the RBC for MeHg.