Linked Life Data

8486610

Source:http://linkedlifedata.com/resource/pubmed/id/8486610

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-6-9
pubmed:abstractText
It is known that nucleoporins, a family of glycoproteins with N-acetylglucosamine that are found in nuclear pore complexes, are essential for nuclear import and export. A major component of the family, p62, was purified from a salt extract of rat liver nuclear envelopes by wheat germ agglutinin-Sepharose affinity chromatography and DEAE-anion exchange HPLC. p62 was purified as a complex with two glycoproteins of 60 and 54 kDa. The presence of the complex was confirmed by gel filtration, glycerol density gradient centrifugation, and cross-linking experiments. The molecular ratio of the 62-, 60-, and 54-kDa components of the complex was estimated to be 1: 1.1 +/- 0.2: 1.7 +/- 0.3 from the intensity of Coomassie Blue staining of SDS-PAGE gels. The complex was stable against 1 M NaCl, 1% Triton X-100, and 2 M urea. The Stokes' radius and sedimentation coefficient of the complex are 8.0 nm and 6.7 S. The molecular mass and frictional ratio of the complex were estimated to be about 231 kDa and 2.0, respectively. p62 and p54 were acidic and neutral proteins, respectively, exhibiting charge heterogeneities, and p60 was assumed to be a basic protein. p60 tended to undergo proteolytic degradation to a 47-kDa fragment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
113
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
377-82
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Purification and characterization of a nuclear pore glycoprotein complex containing p62.
pubmed:affiliation
Department of Biochemistry, Faculty of Science, Niigata University.
pubmed:publicationType
Journal Article