Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1982-10-21
pubmed:abstractText
Mammalian neurofilaments are composed of three subunit polypeptides with approximate molecular weights of 200 000, 150 000, and 70 000 (P200, P150, and P70). These subunits were separated by ion-exchange chromatography in the presence of 8 M urea. The P200 polypeptide was differentially eluted on a diethylaminoethyl (DEAE) column. The P70 and P150 polypeptides obtained after the DEAE column were separable on a hydroxylapatite column. Under neurofilament assembly conditions, only the P70 polypeptide was able to reassemble into an intermediate filament in the absence of the other two polypeptides. The P150 and P70 polypeptides copolymerized into an intermediate filament, only if P70 was present. These results suggest that the P70 polypeptide forms the core of the filament and the other two polypeptides are tightly associated accessory proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3221-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Purification of individual components of the neurofilament triplet: filament assembly from the 70 000-dalton subunit.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.