In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 73, No. 8 ( 1976-08), p. 2659-2663
Abstract:
A small, heat-stable selenoprotein, one of the components of the glycine reductase complex, was labeled with 75Se by growth of Clostridium sticklandii in the presence of Na2 75SeO3. The selenium-containing moiety, which is essential for the biological activity of the protein, was shown to be a selenocysteine residue. It was isolated as its Se-carboxymethyl, Se-carboxyethyl, and Se-aminoethyl derivatives from digests of the pure 75Se-labeled protein that had been reduced and treated with the various alkylating agents prior to hydrolysis. In each instance the 75Se-labeled moiety obtained from an alkylated protein sample and the corresponding alkyl derivative of authentic selenocysteine were indistinguishable. Several studies of the native selenoprotein detected a chromophore (UVmax 238nm) that appeared upon reduction of the protein with KBH4 and rapidly disappeared upon exposure to oxygen. This oxygen-labile chromophore is thought to be the ionized -SeH group of the selenocysteine residue.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.73.8.2659
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
1976
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
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