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ISOLATION OF CYTOKININ NUCLEOSIDASES FROM RIPE TOMATO FRUIT
Author(s) -
ROLLE ROSA,
CHISM GRADY
Publication year - 1986
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1986.tb00105.x
Subject(s) - lycopersicon , cytokinin , riboside , zeatin , tris , chemistry , adenosine , botany , horticulture , biochemistry , biology , auxin , gene
Nucleosidase activity which catalyzes the deribosylation of N 6 (Δ 2 ‐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 N 6 (Δ 2 ‐isopentenyl) adenosine, which was more rapidly degraded than zeatin riboside, when cytokinins were used as substrates for activity measurements.