Isolation of cytokinin nucleosidases from ripe tomato fruit

ABSTRACT Nucleosidase activity which catalyzes the deribosylation of N6 (Δ2‐isopentenyl) adenosine was isolated and partially purified (390‐fold) from ripe tomato fruit (Lycopersicon esculentum Mill). This enzyme system, exhibits pH optima at 6.0 and 7.5 in both Hepes/NaOH and Tris/HCl buffers. 6‐Be...

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Veröffentlicht in:Journal of food biochemistry 1986-12, Vol.10 (4), p.275-283
Hauptverfasser: Rolle, R.S, Chism, G.W. III
Format: Artikel
Sprache:eng
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Zusammenfassung:ABSTRACT Nucleosidase activity which catalyzes the deribosylation of N6 (Δ2‐isopentenyl) adenosine was isolated and partially purified (390‐fold) from ripe tomato fruit (Lycopersicon esculentum Mill). This enzyme system, exhibits pH optima at 6.0 and 7.5 in both Hepes/NaOH and Tris/HCl buffers. 6‐Benzylaminopurine riboside was more rapidly degraded than N6 (Δ2‐isopentenyl) adenosine, which was more rapidly degraded than zeatin riboside, when cytokinins were used as substrates for activity measurements.
ISSN:0145-8884
1745-4514
DOI:10.1111/j.1745-4514.1986.tb00105.x