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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
Cinnamic acid induced changes in reactive oxygen species scavenging enzymes and protein profile in maize (Zea mays L.) plants grown under salt stress.
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Plant growth and development are greatly affected due to changes in environmental conditions and become a serious challenge to scientific people. Therefore, present study was conducted to determine the role of secondary metabolites on the growth and development of maize under abiotic stress
Regulation of glutathione S-transferases of Zea mays in plants and cell cultures.
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An antiserum to glutathione S-transferase (EC 2.5.1.18) from maize (Zea mays L.) responsible for herbicide detoxification has been raised in rabbit. The antiserum was specific to the Mr 26000 subunit of the enzyme from maize seedlings and suspension-cultured cells, and recognized the isoenzymes
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
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
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
High levels of linkage disequilibrium and associations with forage quality at a phenylalanine ammonia-lyase locus in European maize (Zea mays L.) inbreds.
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Forage quality of maize is influenced by both the content and structure of lignin in the cell wall. Phenylalanine Ammonia-Lyase (PAL) catalyzes the first step in lignin biosynthesis in plants; the deamination of L-phenylalanine to cinnamic acid. Successive enzymatic steps lead to the formation of
Husks of Zea mays as a potential source of biopolymers for food additives and materials' development.
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Maize husks, an agricultural and industrial residue generated in a large volume, were investigated as a potential source of useful biopolymers. Thus, their chemical composition was firstly studied, after which two biopolymer products were obtained and characterized. Maize husks were dried and
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
Pyruvate and malate transport and oxidation in corn mitochondria.
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Pyruvate oxidation and swelling in pyruvate solutions by corn (Zea mays) mitochondria were inhibited by alpha-cyano-4-hydroxy-cinnamic acid, an inhibitor of pyruvate transport in animal mitochondria; however, there was no inhibition of pyruvate dehydrogenase activity, and malate and NADH oxidation
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
Biosynthesis of phytoquinones. Biosynthetic origins of the nuclei and satellite methyl groups of plastoquinone, tocopherols and tocopherolquinones in maize shoots, bean shoots and ivy leaves.
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1. By using dl-[ring-(14)C]phenylalanine, dl-[beta-(14)C]phenylalanine, dl-[alpha-(14)C]-tyrosine and dl-[beta-(14)C]tyrosine it was shown that in maize shoots (Zea mays) the nucleus and one nuclear methyl group of each of the following compounds, plastoquinone, gamma-tocopherol (aromatic nucleus)
Toxicokinetics of cinnamaldehyde in F344 rats.
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The toxicokinetic profile of cinnamaldehyde (CNMA) was investigated in Fischer 344 rats. CNMA was found to be unstable in blood. After iv administration, a large fraction of CNMA was immediately oxidized to cinnamic acid. The biological half-life of CNMA after iv administration was found to be 1.7
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
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