Induction of catalytic activity in proteins by lyophilization in the presence of a transition state analogue.
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-non-imprinted 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.
Slade
C J
CJ
Macromolecular Science Department, Institute of Food Research, Earley Gate, Whiteknights Road, Reading, RG6 6BZ, United Kingdom.
Vulfson
E N
EN
D000478:Alkylation; D000818:Animals; D001665:Binding Sites; D001709:Biotechnology; D002384:Catalysis; D002417:Cattle; D005612:Freeze Drying; D066298:In Vitro Techniques; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D011506:Proteins; D012710:Serum Albumin, Bovine