Purification and characterization of l-gulono-γ-lactone oxidase from rat and goat liver
| Autor: | Sidney Udenfriend, Bert M. Tolbert, Morimitsu Nishikimi |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Male
Immunodiffusion Hemeprotein Biophysics Flavin group Biochemistry Cofactor chemistry.chemical_compound Species Specificity L-gulonolactone oxidase Animals Trypsin Sodium dodecyl sulfate Molecular Biology Polyacrylamide gel electrophoresis chemistry.chemical_classification Oxidase test Chromatography biology Goats Rats Molecular Weight Alcohol Oxidoreductases Kinetics Spectrometry Fluorescence Enzyme Liver chemistry Spectrophotometry Microsomes Liver biology.protein Spectrophotometry Ultraviolet |
| Zdroj: | Archives of Biochemistry and Biophysics. 175:427-435 |
| ISSN: | 0003-9861 |
| Popis: | Highly purified preparations of rat and goat l -gulono-γ-lactone oxidase were obtained by a seven-step procedure. Sodium dodecyl sulfate polyacrylamide gel electrophoresis indicated that both enzymes have a monomer molecular weight of 51,000. In the native state, both enzymes demonstrated apparent molecular weights of approximately 500,000, based on gel filtration, indicating that they occur as large aggregates. The absorption spectrum of the goat enzyme showed two peaks, at 455 and 350 nm, due to a falvin prosthetic group; the spectrum of the rat enzyme had an extra peak at 415 nm, suggesting contamination by a heme protein. The absorption maxima of these enzymes at 350 nm were hypsochromically shifted, as compared with normal flavins such as FMN and FAD. Both goat and rat enzyme preparations, when administered to rabbits, produced apparently monospecific antisera. Each enzyme was found to crossreact with the antiserum to the other. |
| Databáze: | OpenAIRE |
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