Linked Life Data

3180465

Source:http://linkedlifedata.com/resource/pubmed/id/3180465

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-11-29
pubmed:abstractText
A minor component of albumin was isolated from normal human serum. It had reduced electrophoretic mobility, reacted normally with specific albumin antiserum and, in contrast to normal albumin, did not bind nickel. Sequence analysis showed that the minor band contained components with Ala-His-Lys- and His-Lys- N-terminal sequences, indicating removal of Asp and Asp-Ala respectively from the parent albumin which was found to have the expected N-terminal sequence of Asp-Ala-His-Lys. Both normal albumin and the minor component had an average of 0.32 residues of glucose bound as fructosamine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0009-8981
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
176
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
179-84
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Characterisation of a slow component of normal human serum albumin.
pubmed:affiliation
Department of Clinical Biochemistry, Christchurch Hospital, New Zealand.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't