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Enzymatic Cross-Linking of Purple Membranes Catalyzed by Bacterial Transglutaminase

Authors :
Schneider F
Fuchsbauer Hl
Pasternack R
Arne Seitz
Norbert Hampp
Source :
Biomacromolecules. 2:233-238
Publication Year :
2001
Publisher :
American Chemical Society (ACS), 2001.

Abstract

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.

Details

ISSN :
15264602 and 15257797
Volume :
2
Database :
OpenAIRE
Journal :
Biomacromolecules
Accession number :
edsair.doi.dedup.....ea12694e93787bdb86d6172d2af81686
Full Text :
https://doi.org/10.1021/bm0056207