Selenite metabolism in rat and human blood.
The binding of selenite, the form of selenium used in the treatment of Keshan disease, to plasma proteins and the role of erythrocytes in this process have been studied. The experiments were carried out by incubating 75Se as selenite with plasma and whole blood in vitro (human and rat) and in vivo (rat) and subsequent fractionation by Sephadex G-150 gel filtration. Human and rat plasma proteins were unable to incorporate selenium from selenite, as shown by the negligible amount present in proteins after incubation of plasma with selenite. The incorporation can be carried out after internalization of selenite by the erythrocytes in a fast, temperature dependent process. Hemoglobin, being the major binding protein for the newly reduced selenium in the erythrocyte, might have a role in the uptake of selenite by erythrocytes. The greater affinity of plasma proteins for the final selenium compound resulting from reduction could be the cause of the efflux. However, this is minimal in the absence of plasma, as is evident from the results obtained from blood reconstituted with saline solution instead of plasma. At least two proteins, one albumin like, probably albumin itself and the other of molecular weight close to or greater than 200,000 in the plasma, are involved in the binding and efflux processes.
Mas
A
A
Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada.
Jiang
J Y
JY
Sarkar
B
B
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D020887:Selenious Acid; D012643:Selenium / Q000097:blood*; D012644:Selenium Radioisotopes; D013696:Temperature
D001798:Blood Proteins; D012644:Selenium Radioisotopes; D020887:Selenious Acid; D012643:Selenium