Linked Life Data

80936

Source:http://linkedlifedata.com/resource/pubmed/id/80936

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1978-11-27
pubmed:abstractText
Myelin basic protein in normal mice is phosphorylated. Since phosphorylation can decrease the net positive charge of the myelin basic protein, this could affect molecular interactions between this protein and other myelin components. In this study 32P incorporation into small and large components of the myelin basic protein was studied in immature and young adult mice and also in Quaking mutants which have a severe myelin deficit. We found a short half-life of 32P in myelin basic protein. The 32P specific activity of myelin basic protein was higher in immature and Quaking mice than in young adult animals. Of the 32P-labeled basic proteins of control and Quaking mice, the small component had a slightly higher specific activity than the large component. Although the small basic protein is quantitatively decreased in Quaking mice, the ratio of specific activity of small to large basic protein is similar in control and Quaking animals. Since Quaking and immature mice have many uncompacted myelin lamellae, these preliminary results suggest that phosphorylation and dephosphorylation could be involved in compaction mechanisms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-2598
pubmed:author
pubmed:issnType
Print
pubmed:volume
100
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
159-70
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
In vivo incorporation of 32P into myelin basic protein from normal and quaking mice.
pubmed:publicationType
Journal Article