tulipa sylvestris/phosphatase

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Purification and characterization of protein phosphatase 2A from petals of the tulip Tulipa gesnerina.

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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

Characterization of four plasma membrane aquaporins in tulip petals: a putative homolog is regulated by phosphorylation.

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We suggested previously that temperature-dependent tulip (Tulipa gesneriana) petal movement that is concomitant with water transport is regulated by reversible phosphorylation of an unidentified plasma membrane intrinsic protein (PIP). In this study, four full-length cDNAs of PIPs from tulip petals

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