• Journal of Life Science
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• v.13 no.6
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• pp.822-828
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• 2003

This study was carried out to investigate the changes of enzymes and micro inorganic nutrients that is associated with flower senescence during flower development in tulip cultivars, ‘Apeldoorn’ and ‘Golden Apeldoorn’. Ribonuclease, peroxidase and protease activities were gradually increased from the stage of early flowering to later Polyphenol oxidase showed the highest activity at stage 5, which the flower was in full bloom indicating that it acts at an initial stage of flower senescence. The protease activity was different in the petal extracts during flower development between the cultivars ‘Apeldoorn’ (red petal) and ‘Golden Apeldoorn’ (yellow petal). This result suggested that protease might relate to pigment biosynthesis in petal of tulip. In contrast to the decrease of inorganic nutrients K, Mn, Zn and P contents during floral development, Ca, Mg and Fe showed the gradual increasement that is similar with ribonuclease, peroxidase and protease. It suggests that they have some interaction during flower senescence.

• BMB Reports
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• v.39 no.6
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• pp.671-676
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• 2006

The holoenzyme of protein phosphatase (PP) from tulip petals was purified by using hydrophobic interaction, anion exchange and microcystin affinity chromatography to analyze activity towards p-nitrophenyl phosphate (p-NPP). The catalytic subunit of PP was released from its endogenous regulatory subunits by ethanol precipitation and further purified. Both preparations were characterized by immunological and biochemical approaches to be PP2A. On SDS-PAGE, the final purified holoenzyme preparation showed three protein bands estimated at 38, 65, and 75 kDa while the free catalytic subunit preparation showed only the 38 kDa protein. In both preparations, the 38 kDa protein was identified immunologically as the catalytic subunit of PP2A by using a monoclonal antibody against the PP2A catalytic subunit. The final 623- and 748-fold purified holoenzyme and the free catalytic preparations, respectively, exhibited high sensitivity to inhibition by 1 nM okadaic acid when activity was measured with p-NPP. The holoenzyme displayed higher stimulation in the presence of ammonium sulfate than the free catalytic subunit did by protamine, thereby suggesting different enzymatic behaviors.