Se-dependent GSH-peroxidase isolated from black sea bass (Centropristis striata).
Black sea bass were injected i.p. with Na2SeO3 (Se-75). A GSH-dependent peroxidase was extracted from the liver via differential centrifugation and gel filtration chromatography. Sea bass liver GSH-peroxidase eluted coincidently with Se-75 and was estimated to have a molecular weight of 72,000. The nature of the selenium-protein bond in the peroxidase was investigated by dialysis vs sodium selenite, glutathione (a sulfhydryl reagent) and alkali. It was concluded that the Se-75 was associated with the peroxidase through a non-sulfhydryl linkage likely to be a C-Se bond. This study confirms that Se is found in a GSH-peroxidase fraction isolated from black sea bass and suggests that Se may play an important role in marine fish.
Braddon-Galloway
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Balthrop
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JE
D000818:Animals; D005399:Fishes / Q000378:metabolism*; D005979:Glutathione Peroxidase / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D011485:Protein Binding; D020887:Selenious Acid; D012643:Selenium / Q000032:analysis / Q000378:metabolism
D005979:Glutathione Peroxidase; D020887:Selenious Acid; D012643:Selenium