Source:http://linkedlifedata.com/resource/pubmed/id/20127149
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2010-3-2
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pubmed:abstractText |
L-histidine, a commonly used buffer for protein formulations, has the potential to oxidize and form multiple byproducts. Previous studies were performed using metal catalyzed oxidation with Fe(2+) or Cu(2+). We re-examined the oxidation of L-histidine under conditions more appropriate to protein formulations.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cations,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Metals,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/tert-Butylhydroperoxide
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1573-904X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
447-56
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pubmed:meshHeading | |
pubmed:year |
2010
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pubmed:articleTitle |
Oxidation of free L-histidine by tert-Butylhydroperoxide.
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pubmed:affiliation |
Amgen Inc., Process and Product Development, Analytical and Formulation Sciences Group, Thousand Oaks, California, 91320, USA.
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pubmed:publicationType |
Journal Article
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