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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
29
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pubmed:dateCreated |
1990-11-21
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pubmed:abstractText |
Selenoprotein P is the second plasma selenoprotein to be purified. It is a glycoprotein and has been shown to be distinct from plasma glutathione peroxidase. This study characterizes selenoprotein P further. Deglycosylation of the protein shifts its migration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis from Mr 57,000 to Mr 43,000, indicating it has a substantial carbohydrate component. Measurement of selenium indicates a selenium content of 7.5 +/- 1.0 atoms/molecule based on a polypeptide weight of 43,000. Amino acid analysis accounts for all the selenium as selenocysteine. The protein is also rich in cysteine (17 residues) and histidine (23 residues). Fragmentation of selenoprotein P by trypsin and by cyanogen bromide produces peptides with varying selenium content. This indicates that selenium-rich regions of the protein exist. The concentration of selenoprotein P determined by radioimmunoassay in serum from control rats is 26.3 +/- 4.5 micrograms/ml and in serum from selenium-deficient rats it is 2.7 +/- 0.8 micrograms/ml. Depletion of selenoprotein P from control serum using an immunoaffinity column indicates that over 60% of serum selenium in the rat is contained in this protein. These results demonstrate that selenoprotein P is the major form of selenium in rat serum. It is the first selenoprotein described which has more than one selenium atom/polypeptide chain.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Cyanogen Bromide,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Selenium,
http://linkedlifedata.com/resource/pubmed/chemical/Selenoprotein P,
http://linkedlifedata.com/resource/pubmed/chemical/Selenoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17899-905
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2211667-Amino Acids,
pubmed-meshheading:2211667-Animals,
pubmed-meshheading:2211667-Cyanogen Bromide,
pubmed-meshheading:2211667-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2211667-Glycoproteins,
pubmed-meshheading:2211667-Male,
pubmed-meshheading:2211667-Molecular Weight,
pubmed-meshheading:2211667-Peptide Fragments,
pubmed-meshheading:2211667-Proteins,
pubmed-meshheading:2211667-Rats,
pubmed-meshheading:2211667-Rats, Inbred Strains,
pubmed-meshheading:2211667-Selenium,
pubmed-meshheading:2211667-Selenoprotein P,
pubmed-meshheading:2211667-Selenoproteins,
pubmed-meshheading:2211667-Trypsin
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pubmed:year |
1990
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pubmed:articleTitle |
Selenium and amino acid composition of selenoprotein P, the major selenoprotein in rat serum.
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pubmed:affiliation |
Department of Medicine, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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