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Induction of catalytic activity in proteins by lyophilization in the presence of a transition state analogue

✍ Scribed by Christopher J. Slade; Evgeny N. Vulfson

Publisher: John Wiley and Sons
Year: 1998
Tongue: English
Weight: 110 KB
Volume: 57
Category: Article
ISSN: 0006-3592
DOI: 10.1002/(sici)1097-0290(19980120)57:2<211::aid-bit9>3.0.co;2-q

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✦ Synopsis

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 ␤-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.

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