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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1982-6-24
|
| pubmed:abstractText |
Kappa-Elastin contains 3.81 lysyl residues per 1000 residues of amino acids. Among these residues, free epsilon-amino groups represent about 16 p. 100, as revealed by guanidination, the buried lysyl residues (buried epsilon-amino groups) represent about 33 p. 100, as revealed by dansylation. After drastic reduction by borohydride, no aldimine bonds were detected and only 6 p. 100 of "deeply buried" amino groups of lysyl residues were detected by a second dansylation. The remaining lysines (about 46 p. 100) are engaged or inaccessible.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0398-7655
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
7
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
37-40
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading | |
| pubmed:year |
1981
|
| pubmed:articleTitle |
Accessibility of epsilon-amino groups of lysine to guanidination in kappa-elastin from bovine ligamentum nuchae.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|