Tyrosinase-catalyzed site-specific immobilization of engineered C-phycocyanin to surface

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Abstract

Enzymatic crosslinking of proteins is often limited by the steric availability of the target residues, as of tyrosyl side chains in the case of tyrosinase. Carrying an N-terminal peptide-tag containing two tyrosine residues, the fluorescent protein C-phycocyanin HisCPC from Synechocystis sp. PCC6803 was crosslinked to fluorescent high-molecular weight forms with tyrosinase. Crosslinking with tyrosinase in the presence of L-tyrosine produced non fluorescent high-molecular weight products. Incubated in the presence of tyrosinase, HisCPC could also be immobilized to amino-modified polystyrene beads thus conferring a blue fluorescence. Crosslinking and immobilization were site-specific as both processes required the presence of the N-terminal peptide in HisCPC.

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Faccio, G., Kämpf, M. M., Piatti, C., Thöny-Meyer, L., & Richter, M. (2014). Tyrosinase-catalyzed site-specific immobilization of engineered C-phycocyanin to surface. Scientific Reports, 4. https://doi.org/10.1038/srep05370

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