Covalent immobilization of proteases and nucleases to poly(methylmethacrylate).
The increased popularity of microfabricated devices formed from plastics such as poly(methylmethacrylate) (PMMA) will benefit from approaches adding (bio)chemical functionality to such surfaces. Here, various proteases and nucleases have been covalently immobilized to PMMA surfaces and shown to retain their enzymatic activity as monitored by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Immobilized enzymes yield structural information at a level equivalent to or exceeding that obtained from conventional homogeneous solution-based approaches. Such an approach could be used to expand the functionality of polymer-based microfabricated devices for biological mass spectrometry.
Rieveschl Laboratories for Mass Spectrometry, Department of Chemistry, University of Cincinnati, PO Box 210172, OH 45221, USA.
Wendy D
WD
Dominick
Beniam T
BT
Berhane
Justin S
JS
Mecomber
Patrick A
PA
Limbach
D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D008969:Molecular Sequence Data; D019904:Polymethyl Methacrylate / Q000737:chemistry*; D012260:Ribonucleases / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D004800:Enzymes, Immobilized; D019904:Polymethyl Methacrylate; D012260:Ribonucleases; D010450:Endopeptidases