Agaricus bisporus tyrosinase—II. Characterization of hydroxylase and dehydrogenase activities

Autor: E. Pessione, C. Polimeni, V. Leone, C. Giunta, G. Papa
Rok vydání: 1994
Předmět:
Zdroj: International Journal of Biochemistry. 26:223-228
ISSN: 0020-711X
DOI: 10.1016/0020-711x(94)90149-x
Popis: 1. 1. Preparative Isoelectric focusing (PIEF) was used to isolate hydroxylasic and dehydrogenasic activities, at different pI. 2. 2. The fraction at pI 4.7 and 4.9 displays a pure dehydrogenase activity (substrate l -DOPA). 3. 3. This fraction did not react with tyrosine, either in the spot-test or in absorption spectra (200–620 nm), and did not exhibit any oxygen consumption. 4. 4. The fraction at pI 4.1 and 4.3 reacted with both l -DOPA and tyrosine as substrate, showing dehydrogenase and hydroxylase activity. 5. 5. The latter activity was confirmed by the oxygen consumption test, showing that molecular oxygen is used to ortho-hydroxylate tyrosine.
Databáze: OpenAIRE