| Autor: |
Seitz, A., Schneider, F., Pasternack, R., Fuchsbauer, H.-L., Hampp, N. |
| Zdroj: |
Biomacromolecules; March 12, 2001, Vol. 2 Issue: 1 p233-238, 6p |
| Abstrakt: |
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. |
| Databáze: |
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