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phenylalanine/картоф
Линкът е запазен в клипборда
Страница 1 от 153 резултата
[Role of L-phenylalanine ammonia lyase in the induced resistance and susceptibility of potato plants].
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Biogenic elicitors (chitosan and its complex with salicylic acid) and an immunosuppressor (laminarin) were shown to increase the activity of L-phenylalanine ammonia lyase (EC 4.3.1.5) and protein synthesis in potato tubers. Laminarin did not decrease L-phenylalanine ammonia lyase activity. It is
Sequential Induction of Phenylalanine Ammonia-lyase and a Lyase-inactivating System in Potato Tuber Disks.
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The light induced synthesis of phenylalanine ammonia-lyase in disks cut from potato tubers is very sensitive to cycloheximide. Synthesis is inhibited 50% in disks cultured on 5 mum cycloheximide instead of water and almost completely in disks aged in the presence of 10 mum inhibitor. Inhibition is
Phenylalanine and tyrosine accumulating cell lines of a dihaploid potato selected by resistance to 5-methyltryptophan.
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The selection and characterization of 5-methyltryptophan (5-MT) resistant cell lines is described in a dihaploid potato, clone H(2)578(007). The frequency of resistant calli was increased by treatment of a cell suspension with N-ethyl-N-nitroso-urea. Two lines, 5-MT-21 and 5-MT-26, accumulated
Immunochemical studies on fluctuation of phenylalanine ammonia-lyase activity in sweet potato in response to cut injury.
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Antibody toward phenylalanine ammonia-lyase (PAL) [EC 4.3.1.5] was obtained by immunization of a rabbit with highly purified PAL. The antibody reacted specifically with RAL, as demonstrated by the Ouchterlony double diffusion test, immunoelectrophoresis, and SDS polyacrylamide gel electrophoresis of
Purification and properties of phenylalanine ammonia-lyase in cut-injured sweet potato.
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L-Phenylalanine ammonia-lyase (PAL) activity was developed in response to cut injury in sweet potato root tissue. The enzyme was purified from tissue incubated for 1 day after slicing by ammonium sulfate fractionation, column chromatographies on L-phenylalanyl Sepharose 4B, phosphocellulose.
Phenylalanine ammonia-lyase and cinnamic acid 4-hydroxylase: Product repression of the level of enzyme activity in potato tuber discs.
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Exogenous supplies of phenylalanne, cinnamic acid and p-coumaric acid can inhibit the appearance of phenylalanine ammonia-lyase (PAL, E.C. 4.3.1.5) activity in potato tuber discs, and exogenous supplies of cinnamic acid and p-coumaric acid can inhibit the appearance of cinnamic acid 4-hydroxylase
Transient Induction of Phenylalanine Ammonia-Lyase and 4-Coumarate: CoA Ligase mRNAs in Potato Leaves Infected with Virulent or Avirulent Races of Phytophthora infestans.
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Infection of potato leaves with the fungal pathogen Phytophthora infestans (Pi) resulted in the rapid stimulation of phenylpropanoid metabolism. Increases in the activities of several mRNAs, including those encoding phenylalanine ammonia-lyase (PAL) and 4-coumarate:CoA ligase (4CL), were detectable
Time course and spatial distribution of phenylalanine ammonia-lyase and peroxidase activity in wounded potato tuber tissue.
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The time course and spatial distribution of wound-induced activities of phenylalanine ammonia-lyase and peroxidase were determined to establish correlations between molecular and cellular aspects of the wound-induced pattern of cell differentiation in potato (Solanum tuberosum L.) tissue. A high
Structure and characterization of a cDNA clone for phenylalanine ammonia-lyase from cut-injured roots of sweet potato.
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A cDNA clone for phenylalanine ammonia-lyase (PAL) induced in wounded sweet potato (Ipomoea batatas Lam.) root was obtained by immunoscreening a cDNA library. The protein produced in Escherichia coli cells containing the plasmid pPAL02 was indistinguishable from sweet potato PAL as judged by
Wound-induced phenylalanine ammonia-lyase in potato tuber tissue. Development of enzyme activity and effects of antibiotics.
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Phenylalanine ammonia-lyase [EC 4.3.1.5.] activity increased rapidly after a 3-hr lag period in potato tuber (Solanum tuberosum L. cv. May Queen) disks incubated in a suitable medium in the dark at 25 degrees. The activity reached a maxinum after incubation for about 40 hr. The effects of
Extensin and Phenylalanine Ammonia-Lyase Gene Expression Altered in Potato Tubers in Response to Wounding, Hypoxia, and Erwinia carotovora Infection.
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Potato (Solanum tuberosum L.) tubers are susceptible to infection by Erwinia carotovora, causal agent of bacterial soft rot, when wounded and subjected to wet, hypoxic environments. The expression of two putative plant defense genes, extensin and phenylalanine ammonia-lyase (PAL), was examined by
Synthesis and removal of phenylalanine ammonia-lyase activity in illuminated discs of potato tuber parenchyme.
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(1) The synthesis and removal of phenylalanine ammonia-lyase (EC 4.3.1.5) in illuminated discs of potato (Solanum tuberosum cv King Edward) tuber tissue has been investigated by density labelling with deuterium (2H) from deuterium oxide (2H2O) followed by centrifugation to equilibrium in a CsC1
Organization of phenylalanine ammonia lyase (PAL), acidic PR-5 and osmotin-like (OSM) defence-response gene families in the potato genome.
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Defence-response (DR) genes are candidates for the genetic functions underlying quantitative resistance to plant pathogens. The organization of three DR gene families encoding phenylalanine ammonia lyase (PAL), acidic PR-(pathogenesis-related) protein 5, and basic PR-5, or osmotin-like (OSM),
Wound-induced phenylalanine ammonia-lyase in potato (Solanum tuberosum) tuber discs. Significance of glycosylation and immunolocalization of enzyme subunits.
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1. Excised discs of potato (Solanum tuberosum) tuber were incubated with [3H]fucose and extracts were prepared and incubated with an antibody to phenylalanine ammonia-lyase. Analysis of the resulting immunoprecipitated proteins by SDS/PAGE showed [3H]mannose- and [3H]fucose-labelled bands with Mr
Density labelling studies of the photocontrol of L-phenylalanine ammonia-lyase in discs of potato (Solanum tuberosum) tuber parenchyme.
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The photocontrol of L-phenylalanine ammonia-lyase (EC 4.3.1.5) activity in discs of potato (Solanum tuberosum) tuber parenchyme has been investigated by density labelling with 2H from 2H2O. Labelling of enzyme was measured by analysis of the equilibrium distribution of enzyme activity in CsCl
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