Interactions of cadmium and selenium in rat plasma in vivo and in vitro.
75Se and 109Cd tracers were used to study the binding of Se and Cd to plasma proteins at various SeO32- doses and times upt to 24 h after the simultaneous subcutaneous administration of SeO32- markedly increased both Se and Cd plasma levels over that in control animals. Gel permeation chromatography of plasma indicated that at all times up to 24 h Cd and Se were bound in an atomic ratio of approx. 1 : 1 in 330 000 and 130 000 dalton fractions. From 4 to 24 h, Cd and Se appeared in the 420 000 dalton fraction, also with an atomic ratio of approx. 1 : 1. The 330 000 dalton molecules appeared to have a maximal binding capacity for the Cd-Se complex at a concentration of approx. 30 mumol/ml of plasma, while the 130 000 and 420 000 dalton molecules show a higher binding capacity. Studies in vitro revealed that SeO32- does not interact directly with Cd and plasma proteins. It is metabolized by erythrocytes to a form that interacts in an atomic ratio of 1 : 1 with Cd to form a protein-bound complex of 130 000 daltons.
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism; D002104:Cadmium / Q000097:blood* / Q000494:pharmacology; D002850:Chromatography, Gel; D004347:Drug Interactions; D066298:In Vitro Techniques; D008297:Male; D051381:Rats; D012643:Selenium / Q000097:blood* / Q000494:pharmacology; D013997:Time Factors
D001798:Blood Proteins; D002104:Cadmium; D012643:Selenium