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trans cinnamic acid/jagung
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Molecular Characterization of a Recombinant Zea mays Phenylalanine Ammonia-Lyase (ZmPAL2) and Its Application in trans-Cinnamic Acid Production from L-Phenylalanine.
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Phenylalanine ammonia-lyase (PAL) is one of the most extensively studied enzymes with its crucial role in secondary phenylpropanoid metabolism of plants. Recently, its demand has been increased for aromatic chemical production, but its applications in trans-cinnamic acid production were not much
Purification and characterization of a glutathione S-transferase from benoxacor-treated maize (Zea mays).
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A glutathione S-transferase (GST) isozyme from maize (Zea mays Pioneer hybrid 3906) treated with the dichloroacetamide herbicide safener benoxacor (CGA-154281) was purified to homogeneity and partially characterized. The enzyme, assayed with metolachlor as a substrate, was purified approximately
The allelochemical trans-cinnamic acid stimulates salicylic acid production and galactose pathway in maize leaves: A potential mechanism of stress tolerance.
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In this study, the effects (5 days) of the secondary metabolite trans-cinnamic acid on maize leaves (Zea mays L.), through a physiological and an untargeted metabolomic approach, were evaluated. A reduction in leaf growth and development accompanied by a decrease in protein content was observed in
The ornamental variety, Japanese striped corn, contains high anthocyanin levels and PAL specific activity: establishing the potential for development of an oral therapeutic.
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Phenylalanine ammonia-lyase [PAL, EC 4.3.1.24 (formerly EC 4.3.1.5)], functions in the plant phenylpropanoid biosynthetic pathway to deaminate the amino acid L-phenylalanine forming trans-cinnamic acid and ammonia. The human inherited metabolic disorder phenylketonuria (PKU) is characterized by an
Solubilized auxin-binding protein : Subcellular localization and regulation by a soluble factor from homogenates of corn shoots.
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Discontinuous sucrose gradient fractionations indicate that the high-affinity auxin binding protein which can be solubilized from the microsomes of coleoptiles and primary leaves of Zea mays L. seedlings is probably located in the endoplasmic reticulum (ER). Since aromatic hydroxylations are
Reversal of Abscisic Acid-Induced Stomatal Closure by trans-Cinnamic and p-Coumaric Acid.
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Abscisic acid (ABA)-induced increase in stomatal diffusive resistance (SDR) in excised leaves of bean (Phaseolus vulgaris L. cv Pencil Pod) and maize (Zea mays L. cv Golden Bantam) is inhibited by low concentrations of trans-cinnamic acid (TCA) (1 micromolar) and p-coumaric acid (PCA) (10
Properties of a Maize Glutathione S-Transferase That Conjugates Coumaric Acid and Other Phenylpropanoids.
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A glutathione S-transferase (GST) enzyme from corn (Zea mays L. Pioneer hybrid 3906) that is active with p-coumaric acid and other unsaturated phenylpropanoids was purified approximately 97-fold and characterized. The native enzyme appeared to be a monomer with a molecular mass of approximately 30
Influence of chemical treatments on glutathione S-transferases of maize with activity towards metolachlor and cinnamic acid.
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The subcellular distribution of glutathione S-transferase (GST) activity extracted from shoots of 3-day-old etiolated seedlings of maize (Zea mays L., Northrup-King 9283 hybrid) and the induction of soluble and membrane-bound GST activity by the safener benoxacor, the herbicide metolachlor and their
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