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Reference type: Journal
Authors: Slade CJ, Vulfson EN
Article Title: Induction of catalytic activity in proteins by lyophilization in the presence of a transition state analogue.
Publication date: 1998
Journal: Biotechnology and Bioengineering
Volume: 57
Issue: (2)
Page numbers: 211-215.
DOI: 10.1002/(SICI)1097-0290(19980120)57:2<211::AID-BIT9>3.0.CO;2-Q

Abstract: The induction of catalytic activity in proteins by lyophilization in the presence of a transition state analogue (biomolecular imprinting) has been attempted. It was shown that proteins which were freeze- dried with N-isopropyl-4-nitrobenzyl-amine (a transition state analogue for the reaction of dehydrofluorination of 4-fluoro-4-[p- nitrophenyl] butan-2-one) displayed higher beta-elimination activity as compared to their-nonimprinted counterparts. It was also found that native bovine serum albumin has a high dehydrofluorination activity towards the above substrate with kinetic parameters rather similar to those of a catalytic antibody prepared by Shokat et al. (1989). A comparison of the kinetic parameters determined in this study with those obtained for analogous catalytic antibodies and imprinted polymers was made. (C) 1998 John Wiley & Sons, Inc

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