Linked Life Data

2076468

Source:http://linkedlifedata.com/resource/pubmed/id/2076468

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1991-4-22
pubmed:abstractText
A rotatable dual-target probe was used for accurate mass measurement in fast atom bombardment mass spectrometry to determine the structures of unknown amino acid residues or post-translationally modified structures in peptides or proteins. The results obtained in measurement of tryptic peptides (with molecular weights of up to 2000) of the A-subunit of vero-toxin I indicated that the mass values obtained are sufficiently accurate and reproducible to allow the generation of the possible elemental compositions for modifications in peptides. By this method, the structural modifications of the N-terminal of a recombinant human leukocyte interferon A and novel halogenated amino acids in sperm-activating peptides from the egg-jelly of sea urchins were determined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0887-6134
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
705-12
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Analysis of post-translational modifications of proteins by accurate mass measurement in fast atom bombardment mass spectrometry.
pubmed:affiliation
Institute for Protein Research, Osaka University, Japan.
pubmed:publicationType
Journal Article