Linked Life Data

9743590

Source:http://linkedlifedata.com/resource/pubmed/id/9743590

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-10-27
pubmed:abstractText
We have isolated a monoclonal antibody, P4B2, which localizes to multiple anchorage junctions, namely, a subset of focal adhesions, the Z-disk of muscle, and neuromuscular junctions. Immunopurification of the antigen to this antibody from chicken brain tissue yielded a complex of three prominent proteins with mobilities of 36, 30, and 18 kDa. Amino acid sequencing of the purified proteins identified the 36-kDa protein as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The other two protein bands were heterogeneous, containing proteins found in the synaptic vesicle fusion core complex. Immunolocalization of P4B2 antigen in developing cultured muscle cells showed that the antigen is incorporated into Z-lines soon after the sarcomeric architecture was positive for alpha-actinin. Together, the data indicate the P4B2 antigen is part of a unique GAPDH-containing protein complex that may be involved in reinforcement of established cytoskeletal structures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-4827
pubmed:author
pubmed:copyrightInfo
Copyright 1998 Academic Press.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
243
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
305-18
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Immunopurification of a sarcomeric junctional protein complex containing GAPDH.
pubmed:affiliation
Department of Biochemistry, University of Illinois, Urbana, Illinois 61801, USA. kmcdonal@uiuc.edu
pubmed:publicationType
Journal Article