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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1981-3-27
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pubmed:abstractText |
A generally applicable strategy has been developed for the primary sequence determination of peptides and proteins containing gamma-carboxyglutamic acid. The intact peptide or protein is either dissolved in, or allowed to come into vapor phase contact with, 0.05 M DCI and then heated in vacuo at 110 degrees C for several hours. Under these conditions gamma-carboxyglutamic acid quantitatively decarboxylates and incorporates two atoms of deuterium per molecule, resulting in the formation of gamma-dideuteroglutamyl residues. Following enzymatic or acidic degradation of the protein the peptide mixture generated is converted (without further isolation of individual peptides) to the N-trifluoroacetylated, O-trimethylsilylated polyamino alcohols and subsequently analyzed by gas chromatography mass spectrometry. Peptide fragments in which gamma-carboxyglutamic acid was present show sequence ions in their mass spectra corresponding to those of glutamic acid, but shifted upwards by 2 amu. This approach has been used to identify the positions of Gla in a tryptic peptide isolated from blood coagulation factor IX, and is currently being employed in the sequence determination of the Gla-containing bone protein osteocalcin.
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pubmed:grant | |
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 |
Apr
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pubmed:issn |
0306-042X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
172-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading | |
pubmed:year |
1980
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pubmed:articleTitle |
Gas chromatographic mass spectrometric sequencing of peptides and proteins containing gamma-carboxyglutamic acid.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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