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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17-18
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pubmed:dateCreated |
2011-6-21
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pubmed:abstractText |
The glycation of human serum albumin (HSA) during diabetes can affect the ability of this protein to bind drugs and small solutes in blood. This study describes the use of (16)O/(18)O-labeling and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to compare the levels of modification that occur throughout HSA under various glycation conditions in vitro. These quantitative studies build on a recent report that has identified the early and advanced glycation products that are formed on such samples of HSA.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1873-3492
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2011 Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
17
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pubmed:volume |
412
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1606-15
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pubmed:meshHeading |
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pubmed:year |
2011
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pubmed:articleTitle |
Quantitative analysis of glycation patterns in human serum albumin using 16O/18O-labeling and MALDI-TOF MS.
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pubmed:affiliation |
Department of Chemistry, University of Nebraska, Lincoln, NE, United States.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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