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Purification of Polyphenol Oxidase from Potato and Investigation of the Inhibitory Effects of Phenolic Acids on Enzyme Activity.

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Polyphenol oxidase (PPO) belongs to the oxidoreductase enzyme family.Here, PPO was purified from potato using Sepharose 4B-L-tyrosine-p-aminobenzoic acid affinity chromatography. It determined the interactions between some phenolic acids and the

A new insight into purification of polyphenol oxidase and inhibition effect of curcumin and quercetin on potato polyphenol oxidase.

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In the literature, the polyphenol oxidase (PPO) enzyme has been purified a many times via Sepharose 4B-l-tyrosine-p-aminobenzoic acid affinity column. In order to study PPO purification efficiency, 2-aminophenol and 4-aminophenol were applied as a spacer arm to CNBr-activated Sepharose 4B. The

l-Phenylalanine Ammonia-Lyase (Maize): Evidence for a Common Catalytic Site for l-Phenylalanine and l-Tyrosine.

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l-Phenylalanine ammonia-lyase (E.C. 4.3.1.5) from maize is active with l-tyrosine and l-phenylalanine and exhibits atypical Michaelis-Menten kinetics with both substrates. With phenylalanine as a substrate, the pH optimum is 8.7 and with tyrosine, 7.7. The estimated Km at high substrate

Purification and characterization of p-coumaroyl-D-glucose hydroxylase of sweet potato (Ipomoea batatas) roots.

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p-Coumaroyl-D-glucose hydroxylase in sweet potato (Ipomoea batatas Lam.) has been purified to apparent electrophoretic homogeneity using a combination of anion-and cation-exchange, hydrophobic and gel filtration chromatography. The purified enzyme was a monomer with a molecular weight of 33,000 and

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.

Proteinase activity in potato plants.

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Several vegetative tissues of potato plants were screened for proteinase activity. Both endopeptidase and exopeptidase activities were investigated using gelatin and L-amino acid-4-nitroanilides (benzoyl-L-arginine-4-nitroanilide/BAPA, glutaryl-L-phenyl-alanine-4-nitroanilide/GLUPHEPA,

First Report of Potato Scab Caused by Streptomyces turgidiscabies in China.

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Potato scab, caused by several plant pathogenic Streptomyces species, is known to occur in potato-planting areas worldwide. Symptoms of disease on potato tubers are shallow, raised, or pitted corky lesions (2). In 1998, Streptomyces turgidiscabies was reported as a new potato scab pathogen from

L-Tyrosine beta-naphthylamide is a potent competitive inhibitor of tyramine N-(hydroxycinnamoyl)transferase in vitro.

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L-Tyrosine beta-naphthylamide, a synthetic substrate designed to measure tyrosine aminopeptidase activity, is a potent inhibitor of hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)transferase (THT) purified from elicited tobacco cell-suspension cultures. The inhibition is competitive, with the

Beta-1,3-glucooligosaccharide induced activation of four enzymes responsible for N-p-coumaroyloctopamine biosynthesis in potato (Solanum tuberosum cv.) tuber tissue.

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Potato tuber disks, when treated with laminarin, a beta-1,3-glucooligosaccharide from Laminaria digitata, accumulate a hydroxycinnamoyl amide compound, N-p-coumaroyloctopamine (p-CO). The biosynthesis of p-CO was investigated by feeding experiments, in order to show that the precursors of

Purification and Characterization of a Potato Tuber Acid Phosphatase Having Significant Phosphotyrosine Phosphatase Activity.

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The major acid phosphatase (APase) from potato (Solanum tuberosom L. cv Chiefton) tubers has been purified 2289-fold to near homogeneity and a final O-phospho-L-tyrosine (P-Tyr) hydrolyzing specific activity of 1917 [mu]mol Pi produced min-1 mg-1 of protein. Nondenaturing polyacrylamide gel

Rapid purification and N-terminal sequencing of a potato tuber cyclic nucleotide binding phosphatase.

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A high affinity cyclic nucleotide binding phosphatase was purified to homogeneity from potato tubers by a rapid procedure involving batchwise elution from carboxymethylcellulose and gel filtration. The phosphatase has a molecular weight of 28,000 as estimated from both SDS-PAGE and gel filtration.

Transformation of L-tyrosine to L-dopa by a novel fungus, Acremonium rutilum, under submerged fermentation.

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The present study deals with the transformation of L-tyrosine to L-dopa by Acremonium rutilum, a fungal tyrosinase producer, isolated from decomposed banana stud. This appears to be the first report on A. rutilum as a polyphenoloxidase producer with both cresolase and catecholase activity. Enriched

Studies on enzymic browning of potatoes (Solanum tuberosum). III. Kinetics of potato phenoloxidase (EC 1.14.18.1 monophenol, dihydroxyphenylalanine: oxygen-oxidoreductase).

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From initial velocity studies a sequential mechanism for the reactions catalysed by phenoloxidase from potatoes is indicated. The data are in accordance with an ordered addition of oxygen and phenolic substrate to the enzyme, with oxygen being the first substrate bound at thermodynamic equilibrium.

A two-component affinity chromatography purification of Helix pomatia arylsulfatase by tyrosine vanadate.

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The inhibition of Helix pomatia arylsulfatase by the synergistic combination of N-acetyl-l-tyrosine ethyl ester and vanadate has been extended to affinity chromatography for purification. In the presence of vanadate, l-tyrosine ethyl ester (TEE), immobilized on CH-Sepharose 4B retained arylsulfatase

Degradation of tyrosinase induced by phenylthiourea occurs following Golgi maturation.

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Tyrosinase, the rate-limiting enzyme of melanin synthesis, is a di-copper metalloprotein that catalyzes the conversion of L-tyrosine to L-DOPAquinone. Phenylthiourea (PTU) is a well-known inhibitor of tyrosinase and melanin synthesis and is known to interact with sweet potato catechol oxidase, an

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