Linked Life Data

8227200

Source:http://linkedlifedata.com/resource/pubmed/id/8227200

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1993-12-22
pubmed:abstractText
A polyclonal antibody was raised to the C-terminal region of fission yeast BiP. The use of this antibody for immunoprecipitation, western blotting and immunofluorescence has confirmed and extended the observations made previously with an epitope-tagged BiP molecule. A fraction of BiP protein is glycosylated in Schizosaccharomyces pombe cells. Pulse-chase experiments showed that this modification occurs rapidly upon synthesis and that the extent of glycosylation does not then change with time. BiP protein is induced by elevated temperatures and by treatment with tunicamycin. The antibody cross-reacts with proteins of similar molecular weight in the yeasts Kluyveromyces lactis and Schizosaccharomyces japonicus. Immunofluorescence of BiP has been used to follow the behaviour of the ER and in particular the nuclear envelope through the cell cycle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
105 ( Pt 4)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1115-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The BiP protein and the endoplasmic reticulum of Schizosaccharomyces pombe: fate of the nuclear envelope during cell division.
pubmed:affiliation
Membrane Molecular Biology Laboratory, Imperial Cancer Research Fund, London, UK.
pubmed:publicationType
Journal Article, Comparative Study