BIOLOGICAL ACTIVITY OF ENZYMES IMMOBILIZED ON SILANIZED SOLID SUBSTRATES EITHER DIRECTLY OR THROUGH PHOSPHOLIPID CROSS-LINKERS

Authors
  1. Kallury, K.M.R.
  2. Thompson, M.
Corporate Authors
Defence Research Establishment Suffield, Ralston ALTA (CAN);Toronto Univ, Toronto ONT (CAN) Dept of Chemistry
Abstract
Two omega-carboxyalkyl silyloxy-substituted silica surfaces were prepared with six and ten carbon spacer chain length, respectively. The carboxylic moieties on these surfaces were either directly coupled to urease in the presence of a diimide or were first activated with N-hydroxy succinimide or carbonyldiimidazole and then linked to urease, to afford two sets of silicon/silane-enzyme surfaces. Phosphatidylcholines with a protected hydroxyl on the terminal carbon of the sn-1 chain and a protected amino moiety on the terminal carbon of the sn-2 chain were synthesized, in order to effect covalent binding to both silanized surfaces and to urease. The amino group on the lipid was linked to the carboxyl of the silanized surface, while the hydroxyl on the other chain was oxidized to a carboxyl and bound to the amino groups on urease. Two sets of silica/silane-lipid-enzyme surface structures were thus produced. TRUNCATED
Report Number
DRES-CR-30-91 — Contract Report
Date of publication
01 Jan 1991
Number of Pages
49
DSTKIM No
91-03377
CANDIS No
70568
Format(s):
Hardcopy;Originator's fiche received by DSIS

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