Preparation of Aldehyde Oxidase in Its Native and Deflavo Forms
Year: 1974
Type: article
Abstract: Aldehyde oxidase (EC 1.2.3.1) has been purified by a modification of a previously reported procedure and the FAD prosthetic group has been removed by treatment with calcium chloride and calcium acetate. The deflavo enzyme so obtained is devoid of N1-methylnicotinamide oxygen reductase activity but can be reconstituted by a short incubation with FAD. The different activities of native and deflavo enzymes using oxygen, cytochrome c, potassium ferricyanide, nitro blue tetrazolium, dichlorophenolindophenol, and FAD as electron acceptors and N1-methylnicotinamide as substrate are compared.
Source: Journal of Biological Chemistry
Authors: Umberto Branzoli, Vincent Massey
Institution: University of Michigan
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1577554258