Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1980-10-24
|
| pubmed:abstractText |
It is well established that during the isothiocyanate degradation of proteins a gradual increase of the level of all thiohydantoin derivatives of amino acids occurs, which progressively obscures the sequential identification of the significant N-terminal amino acids. The major cause for this has been shown to be due to a hitherto unknown specific cleavage at aspartic acid residues in anhydrous heptafluorobutyric acid and to a lesser extent, the N leads to O shift in peptide bonds involving hydroxyamino acids. Measures to reduce the susceptibility of the peptide bonds at these sites are described.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0018-4888
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
361
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
943-52
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading | |
| pubmed:year |
1980
|
| pubmed:articleTitle |
Nature and extent of peptide bond cleavage by anhydrous heptafluorobutyric acid during Edman degradation.
|
| pubmed:publicationType |
Journal Article
|