Some properties of active and latent catechol oxidase of mushroom

• Autorzy: Czapski J
• Języki publikacji: EN

Abstrakty

EN

Latent form of mushroom catechol oxidase was activated by 0.1% sodium dodecyl sulfate (SDS). Catalytic power of the latent form, calculated from the kinetic parameters was 1.8 times higher than that of active one. Salicyl hydroxamic acid (SHAM) appeared as a powerful inhibitor for both active and latent forms of catechol oxidase. However, in the range of 150-250 μM SHAM the inhibitory effect for active catechol oxidase was significantly higher than that for the latent one. Non-competitive and irreversible characteristics of inhibition of latent and active catechol oxidase was calculated from kinetic data. Electrophoretic analysis followed by scanning of the gels was used. The spots' absorbance was determined from a computer image of the isoenzyme band patterns. It allowed us to estimate gels quantitatively. Presence of one additional clearly defined slow moving isoform of SDS-activated catechol oxidase, differed in the respect of 3 bands for the active and 4 bands for the total.

PL

Aktywowano formę utajoną oksydazy katecholowej pieczarek (Agaricus bisporus) 0,1 % roztworem siarczanu dodecylo - sodowego (SDS). Siła katalityczna formy utajonej była 1,8 razy większa niż formy aktywnej. Stwierdzono, że kwas salicylohydroksy- amowy (SHAM) jest silnym inhibitorem aktywności obydwu form oksydazy katecholowej. Działanie SHAM w zakresie stężeń 150 - 250 μM bylo znacznie efektywniejsze dla formy aktywnej niż utajonej. Stwierdzono niekompetencyjny i nieodwracalny charakter inhibicji aktywności przez SHAM obydwu form enzymatycznych. Rozdział elektroforetyczny i następnie „skaningowanie" żeli pozwoliło na uzyskanie obrazu komputerowego wzoru izoenzymatycznego oraz na jego ilościową ocenę. Obecność dodatkowego izoenzymu we wzorze izozymowym obydwu form: aktywnej i utajonej łącznie (4 frakcje), odróżniało go od wzoru izoenzymatycznego tylko formy aktywnej (3 frakcje).

Słowa kluczowe

EN

active catechol oxidase; latent form; Agaricus bisporus; isoenzyme pattern; catechol oxidase; mushroom

• Wydawca: -
• Czasopismo: Acta Agrobotanica
• Rocznik: 1999
• Tom: 52
• Numer: 1-2
• Opis fizyczny: p.139-147,fig.

Twórcy

autor

Czapski J

• Research Institute of Vegetable Crops, Konstytucji 3-Maja 1-3, 96-100 Skierniewice, Poland

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