Linked Life Data

11749178

Source:http://linkedlifedata.com/resource/pubmed/id/11749178

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-12-25
pubmed:abstractText
It was found that bacterial transglutaminase (TGase) facilitates selective cross-linking of bacteriorhodopsin (BR) in purple membrane (PM) form under mild conditions. Fluorescent probes were used to detect that the membrane protein BR may act as a glutamine donor as well as a lysine donor for TGase. The binding sites were determined to be Gln-3 as the reactive glutamine, and Lys-129 is the corresponding lysine residue. Upon incubation of PM with TGase, cross-linking of PM patches can be achieved without an additional spacer molecule. To our knowledge, this is the first time that an intermembrane cross-linking of membrane-bound proteins is reported. Furthermore, this finding may provide the ability to achieve covalent linkage of complete purple membrane patches to synthetic polymers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1525-7797
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
233-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Enzymatic cross-linking of purple membranes catalyzed by bacterial transglutaminase.
pubmed:affiliation
Institute for Physical Chemistry, University of Marburg, D-35032 Marburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't