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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1985-8-28
|
| pubmed:abstractText |
A simple, rapid technique is presented for preferential cleavage at aspartylprolyl peptide bonds. The method is based upon the fact that these peptide bonds are 8-20-fold more labile in 0.015 N HCl at 100-110 degrees than other aspartyl-X or X-aspartyl peptide bonds. The method has proven effective in the cleavage of several peptides from pig kidney fructose-1,6-bisphosphatase and should facilitate sequence analysis of proteins that contain aspartyl-prolyl linkages.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0367-8377
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
25
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
542-6
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1985
|
| pubmed:articleTitle |
Preferential cleavage at aspartyl-prolyl peptide bonds in dilute acid.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|