Electrosynthetic immobilisation of proteins for bioanalysis

D J Walton, C J Campbell, P G Richards, J Heptinstall, Colin Campbell

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Use of electrosynthetic methodology allows the production of hen egg-white lysozyme (HEWL) either mononitrated at tyrosine 23 or bisnitrated at tyrosines 20 and 23, but never nitrated at tyrosine 53, This is a different sequence from that obtained by the chemical nitrating agent tetranitromethane, and when reduced by dithionite, the selectively modified enzyme can be anchored at pH 5 via the unique aromatic amino group to magnetic beads or other suitable matrices. HEWL so immobilised loses less than 10% of cell-wall lytic activity compared with the approximately 50% loss of activity when immobilised by conventional methodology at pH 9 via essentially random reaction at lysine residues and other functionalities which are nucleophilic at this pH, This result offers promise as a general method for selective protein immobilisation in biosensors and similar applications. (C) 1998 John Wiley & Sons, Ltd.

Original languageEnglish
Pages (from-to)101-105
Number of pages5
JournalAdvanced Materials for Optics and Electronics
Volume8
Issue number2
Publication statusPublished - 1998

Keywords / Materials (for Non-textual outputs)

  • biosensor
  • protein immobilisation
  • protein modification
  • electrochemistry
  • nitrotyrosine
  • LYSOZYME

Fingerprint

Dive into the research topics of 'Electrosynthetic immobilisation of proteins for bioanalysis'. Together they form a unique fingerprint.

Cite this