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Se-dependent GSH-peroxidase isolated from black sea bass (Centropristis striata)

Authors :
J.E. Balthrop
Sylvia Braddon-Galloway
Source :
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology. 82:297-300
Publication Year :
1985
Publisher :
Elsevier BV, 1985.

Abstract

1. Black sea bass were injected i.p. with Na 2 SeO 3 (Se-75). A GSH-dependent peroxidase was extracted from the liver via differential centrifugation and gel filtration chromatography. 2. Sea bass liver GSH-peroxidase eluted coincidently with Se-75 and was estimated to have a molecular weight of 72,000. 3. 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. 4. 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.

Details

ISSN :
03064492
Volume :
82
Database :
OpenAIRE
Journal :
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology
Accession number :
edsair.doi.dedup.....825f256c5082f8ff8038ab25a481a5d3
Full Text :
https://doi.org/10.1016/0742-8413(85)90166-5