|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
Pt 5
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|
pubmed:dateCreated |
2010-9-6
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|
pubmed:abstractText |
In human serum, a portion of homocysteine (Hcy) exists as an N-linked form to the epsilon-amino group of protein lysine residues. N-homocysteinylated proteins differ structurally and functionally from native proteins. The present study strives to develop detection and potential semi-quantification methods for N-homocysteinylated apolipoprotein AI (N-Hcy-apoAI) in human serum.
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pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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|
pubmed:month |
Sep
|
|
pubmed:issn |
1758-1001
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|
pubmed:author |
|
|
pubmed:issnType |
Electronic
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|
pubmed:volume |
47
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
453-9
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|
pubmed:meshHeading |
|
|
pubmed:year |
2010
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|
pubmed:articleTitle |
Identification of N-homocysteinylated apolipoprotein AI in normal human serum.
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|
pubmed:affiliation |
Analytical Laboratory Chemistry, Graduate School of Health Care Sciences, Tokyo Medical and Dental University, Tokyo.
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|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
