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Toxic doses of Selenium (Se) (12.5 and 37.5 micro moles/Kg egg wt.) administered to 14 day old chick embryos reduced the level of lipid peroxides (LPO) significantly both in hepatic and brain tissues. However, the LPO formation was inhibited maximally at early hours after exposure (3 h and 6 h) and it was gradually increased thereafter to normal levels by 48 h. Further, the effect of Se on some of the antioxidant enzymes like glutathione peroxidase (GPx), glutathione transferase (GST), glutathione reductase (GR), superoxide dismutase (SOD) and catalase were studied. In hepatic tissues GPx, GST and SOD activities were increased at 6 h post treatment with no change in the activities of GR and catalase. However, at 48 h GST and catalase activities were found to be increased, while GPx, GR and SOD activities were not affected. In brain at 6 h increase in the activities of GPx, GST, GR and SOD and no change of catalase were observed. At 6 h glutathione (GSH) levels were reduced in both hepatic and brain tissues. Our results suggest that the elevated levels of antioxidant enzymes at early hours were successful in bringing LPO levels back to normal.

Effect of different concentrations of selenium (Se) on heme biosynthesis was studied at different developmental stages of chick embryo. The first rate limiting enzyme ALA-synthase (ALA-S; E.C.2.3-1.37) activity was enhanced by selenium, while hepatic and blood ALA-dehydratase activity (ALA-d; E.C.3.2.1.24) was decreased. Hepatic and blood free-sulfhydryl (-SH) group contents were significantly decreased by Se. Further, hepatic aminolevulinic acid (ALA) and total blood porphyrin levels were enhanced and hepatic heme levels were depleted by selenium exposure. Heme biosynthesis was maximally inhibited in the E4 (4th day injected embryos) when compared to later periods.

Distribution study using 75Se shows that maximum accumulation was in liver tissues after 24h of 75Se administration. Induction of selenium binding protein (Se-P) in hepatic tissues of chick embryo was observed. Chick embryo hepatic Se-P was isolated after 24h of 75Se treatment using Sephadex G-75 column chromatography. Fractions of induced protein shows the presence of maximum concentration of 75Se. This induced protein was found to have an approximate molecular weight of 56 KD on molecular sieve. It also showed an absorbance maxima at 254 nm, which indicates the presence of high concentrations of sulphydryl groups.

A few selected indices of heme biosynthesis have been studied in liver and blood from chick embryos receiving different concentrations of selenium of toxicological significance 12.5, 25 and 37.5 mumoles/Kg egg.Wt.). The first rate limiting enzyme Aminolevulinic acid synthetase activity was enhanced by selenium treatment under both IN VIVO and IN VITRO conditions, while hepatic ALA dehydratase activity was unaltered. Hepatic and blood free sulfhydryl (-SH) group contents were significantly decreased by selenium. In accordance with these results, blood aminolevulinic acid dehydratase (ALA dehydratase) and hepatic ferrochelatase, both the sulfhydryl group requiring enzymes, were significantly inhibited. Further, hepatic ALA, total blood porphyrin levels were enhanced and hepatic heme levels were depleted by selenium exposure. These results suggest selenium as a novel regulator of heme biosynthesis by altering the activities of sulfhydryl group requiring enzymes of chick embryos.

5-Aminolevulinic acid, porphyrin and chlorophyll contents as well the activities of 5-aminolevulinic acid dehydratase and PBG deaminase were studied in selenium treated mung bean seedlings. Selenium had no effect on 5-aminolevulinic acid synthetic ability but inhibited 5-aminolevulinic acid dehydratase and PBG deaminase activities. Further, it was observed that selenium induced accumulation of protoporphyrin-IX and Mg-protoporphyrin ester and decreased chlorophyll levels in both light and dark-grown seedlings. The results suggest the possible regulatory role of selenium on chlorophyll synthesis by interacting with sulfhydryl containing enzymes 5-aminolevulinic acid dehydratase and porphobilinogen deaminase.