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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
18
|
| pubmed:dateCreated |
1992-1-22
|
| pubmed:abstractText |
Peptides derived from enzymatic digestions (cathepsin D and trypsin) were characterized and amino acid sequences determined by using their LC/MS spectra. A Frit-FAB interface that produces extensive peptide fragmentation and permits amino acid sequencing at the low picomole level is described for a model antigen, Staphylococcus aureus nuclease (Nase), and an enzyme of unknown structure, yeast aminopeptidase B. The amino acid sequences of peptides derived from digestion of Nase with cathepsin D (a relatively nonspecific endoprotease) were readily deduced and have provided insights into the nature of antigen processing. Frit-FAB LC/MS spectra of the Nase peptides contained a sufficient number of fragment ions to conclusively identify peptides with a mass below 2000 Da. Capillary LC/MS provided a means for the separation and identification of these enzymatically derived peptides in a fraction of the time that would have been required by gas-phase Edman sequence analysis. The optimized Frit-FAB experiment was consequently evaluated for the partial characterization of aminopeptidase B recently purified to homogeneity from Saccharomyces cerevisiae. Sequence-specific ions observed in the Frit-FAB mass spectra of these tryptic peptides were identical with those commonly observed in high-energy collision-induced dissociation (CID) spectra and included side-chain fragment ions that differentiated leucine from isoleucine. These fragment ions were used to deduce entire amino acid sequences for several of the tryptic peptides.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0003-2700
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
63
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1978-83
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1991
|
| pubmed:articleTitle |
Optimization of the fragmentation in a frit-fast atom bombardment ion source for the sequencing of peptides at the picomole level.
|
| pubmed:affiliation |
Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|