Linked Life Data

7641295

Source:http://linkedlifedata.com/resource/pubmed/id/7641295

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-9-18
pubmed:databankReference
pubmed:abstractText
Antibodies against pokeweed agglutinin binding proteins isolated from F9 embryonal carcinoma cells were used to screen a lambda gt11 expression library constructed from the cells. A cDNA clone thus obtained encoded a novel calcium binding protein of 140 kDa (CBP-140). Antibodies raised against the CBP-140 fusion protein stained a 140 kDa band in extracts not only from F9 cells but also from various mouse organs. A calcium blot experiment using CBP-140 fusion protein verified the calcium binding property of the protein. In the partial amino acid sequence so far clarified (652 amino acid residues) we could not detect EF-hand, but could detect contiguous acidic amino acids, which may serve as a calcium-binding site. CBP-140 showed homology with 70-kDa heat shock protein, though it was not induced by heat shock treatment. Localization of CBP-140 in endoplasmic reticulum was shown by indirect immunofluorescence staining and also by subcellular fractionation. Amino acid sequence of CBP-140 contains a carboxyl-terminal Asn-Asp-Glu-Leu (NDEL) sequence, which resembles Lys-Asp-Glu-Leu (KDEL) sequence, a signal to retain the resident proteins in endoplasmic reticulum; NDEL sequence may indeed play a similar role.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0386-7196
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-41
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
CBP-140, a novel endoplasmic reticulum resident Ca(2+)-binding protein with a carboxy-terminal NDEL sequence showed partial homology with 70-kDa heat shock protein (hsp70).
pubmed:affiliation
Department of Biochemistry, Faculty of Medicine, Kagoshima University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't