Linked Life Data

18370025

Source:http://linkedlifedata.com/resource/pubmed/id/18370025

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-3-28
pubmed:abstractText
Pancreatic zymogen granules (ZGs) are specialized for digestive enzyme storage and regulated secretion in exocrine pancreas and are a classical model for studying secretory granule function. To understand the function of this organelle, we have conducted a proteomic study to identify the ZG membrane (ZGM) proteins from ZGs purified by Percoll gradient centrifugation. By combining multiple separation strategies including two-dimensional gel electrophoresis and two-dimensional HPLC with tandem mass spectrometry, we identified 101 proteins from purified ZGMs including a large number of proteins previously unknown on ZGMs. To distinguish intrinsic membrane proteins from soluble and peripheral membrane proteins, a quantitative proteomics strategy was used to measure the enrichment of intrinsic membrane proteins through the purification steps by labeling crude, KBr-, and Na(2)CO(3)-washed ZGMs with multiplexed isobaric tags (iTRAQtrade mark), 114, 116, and 117, respectively. The proteins with 117:114 ratios greater than one correlated well with intrinsic membrane proteins that contain either known or predicted transmembrane domains.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1064-3745
pubmed:author
pubmed:issnType
Print
pubmed:volume
432
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
275-87
pubmed:dateRevised
2008-9-11
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Purification and proteomics analysis of pancreatic zymogen granule membranes.
pubmed:affiliation
Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural