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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
|
| pubmed:dateCreated |
1985-7-12
|
| pubmed:abstractText |
By a combination of chromatographic methods, we have obtained in an apparently homogeneous state the 24 kDa "major myelin proteolipid" (MMPL) and the 20 kDa "myelin proteolipid" (DM-20). Contrary to a commonly held view, the second one is not a conformationally different form of its major companion, as it differs markedly by its amino-acid composition, its electrophoretic behaviour after performic acid oxidation, and the results of tryptic digestion; however, they are obviously very closely related, as shown by the selective cleavages at the level of methionines and tryptophanes. These results are most simply interpreted by a single deletion in DM-20 of the hydrophilic fragment 100-140 of the (known) structure of the 24 kDa proteolipid. Lees' hypothesis of a deletion of fragment 197-267 cannot be retained.
|
| pubmed:language |
fre
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0764-4469
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
300
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
241-6
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading | |
| pubmed:year |
1985
|
| pubmed:articleTitle |
[Structural data on the myelin proteolipid of apparent molecular weight 20 kDa (DM-20)].
|
| pubmed:publicationType |
Journal Article,
English Abstract
|