Linked Life Data

6366787

Source:http://linkedlifedata.com/resource/pubmed/id/6366787

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-4-12
pubmed:abstractText
Aminomalonic acid (Ama) has been isolated from proteins of Escherichia coli and human atherosclerotic plaque. The presence of Ama has important biological implications because the malonic acid moiety potentially imparts calcium binding properties to protein. Ama was obtained by anaerobic alkaline hydrolysis and identified by chromatographic behavior, quantitative acid-mediated decarboxylation to glycine, and unambiguous gas chromatographic/mass spectral detection. The chromatographic, chemical, and mass spectral properties of naturally occurring Ama were identical to those of the synthetic compound. Amino acid analysis and GC/mass spectrometry also revealed the presence of beta-carboxyaspartic acid and gamma-carboxyglutamic acid in the base hydrolysate of human atherosclerotic plaque. The ratio of Ama to beta-carboxyaspartic acid to gamma-carboxyglutamic acid was 20:1:10, and the quantity of Ama per 1,000 glycine residues was 0.2. Ama is a relatively unstable, minor amino acid in complex structures such as bacteria or tissues. This may explain why it has escaped detection previously, despite intensive investigation.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
722-5
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Aminomalonic acid: identification in Escherichia coli and atherosclerotic plaque.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't