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cinnamic acid 4 hydroxylase/компир
Врската е зачувана во таблата со исечоци
9 резултати
Studies on the induction of cinnamic acid 4-hydroxylase in potato tuber.
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The change in activity of cinnamic acid 4-hydroxylase (CA4H) in potato parenchyma tissue exposed to various conditions has been examined. Maximum induction of CA4H activity was obtained at 18 hr of incubation. Though CA4H induction can occur in dark, over 100% increase in enzyme activity was
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
Studies on cinnamic acid-4-hydroxylase from wounded potato tissue: isolation and characterization of cinnamic acid-4-hydroxylase activation factor.
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Cinnamic acid-4-hydroxylase activation factor has been found to be located in the supernatant fraction of wounded potato tissue homogenate in phosphate buffer. The factor has been purified to homogeneity as judged by SDS polyacrylamide gel electrophoresis, by heat treatment on boiling water-bath for
Identification of a non-microsomal cinnamic acid 4-hydroxylase from potato tuber (S. tuberosum) and its partial purification.
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The cytoplasmic localisation of cinnamic acid 4-hydroxylase (CA4H) has been shown by isolation and subcellular fractionation of the enzyme in Hepes buffer. The enzyme was purified by ammonium sulphate fractionation followed by AcA-34 molecular sieve chromatography. The enzyme existed as a high
Phenylalanine ammonia-lyase and cinnamic acid 4-hydroxylase: Characterisation of the concomitant changes in enzyme activities in illuminated potato tuber discs.
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Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) and cinnamic acid 4-hydroxylase (CA4H, EC 1.14.13.11) undergo concomitant increases in activity after a 2 h lag following disc preparation and illumination. The increases in PAL and CA4H activity can be inhibited by actinomycin-D, cordycepin and
Properties of a Mixed Function Oxygenase Catalyzing Ipomeamarone 15-Hydroxylation in Microsomes from Cut-Injured and Ceratocystis fimbriata-Infected Sweet Potato Root Tissues.
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Ipomeamarone 15-hydroxylase activity was found in a microsomal fraction from cut-injured and Ceratocystis fimbriata-infected sweet potato (Ipomoea batatas Lam. cv. Norin No. 1) root tissues and its optimum pH was 8.0. The enzyme reaction required O(2) and NADPH. The K(m) values calculated for
Polarity of Production of Polyphenols and Development of Various Enzyme Activities in Cut-injured Sweet Potato Root Tissue.
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Investigation of polyphenol production in cut-injured sweet potato (Ipomoea batatas Lam. cv. Kokei 14) roots by histochemical and quantitative methods showed that polyphenols were produced in striking amounts in the proximal side of the tissue pieces (2 cm thick), but only in small amounts in cells
The effects of infection by Phytophthora infestans on the control of phenylpropanoid metabolism in wounded potato tissue.
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During the first 24 h of in vitro incubation of excised potato tuber (Solanum tuberosum L.) discs, the appearance of phenylalanine ammonia-lyase (PAL; EC 3.4.1.5) and the accumulation of chlorogenic acid are both stimulated by infection with Phytophthora infestans (Mont.) de Bary. Whereas in control
The phenyl propanoid pathway enzymes in Solanum tuberosum exist as a multienzyme complex.
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The elution profile of the core sequence enzymes of the phenyl propanoid pathway, namely phenyl alanine ammonia lyase, t-cinnamic acid 4-hydroxylase and p-coumaryl CoA ligase, on AcA 34 column suggested the existence of a high molecular form (P1) and a low molecular form (P2) for all the three
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