Characterization of free and immobilized amine oxidases.
Bovine plasma amine oxidase was covalently bound to CH-Sepharose 4B by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride. The immobilized enzyme showed no significant change in specific activity when spermidine was the substrate, while the enzyme affinity toward benzylamine and propylamine increased significantly. Similarly, the pig kidney diamine oxidase physically adsorbed to Con A-Sepharose showed large changes in affinity toward substrates such as p-dimethylaminoethylbenzylamine with respect to the native enzyme. These changes are discussed in terms of active site modification as a consequence of the enzyme immobilization.
Stevanato
R
R
Department of Physical Chemistry, University of Venice, Italy.
Porchia
M
M
Befani
O
O
Mondovi
B
B
Rigo
A
A
D006631:Amine Oxidase (Copper-Containing) / Q000032:analysis*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000032:analysis* / Q000097:blood; D013095:Spermidine / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine
D004800:Enzymes, Immobilized; D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors; D013095:Spermidine