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tryptophan/kartafla

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The affinity of potato tuber starch-branching enzyme-I (PSBE-I) for various linear malto-oligosaccharides, cyclodextrins, (CDs) and macromolecular alpha-glucans was investigated by alpha-glucan induced fluorescence quenching of intrinsic PSBE-I tryptophan residues and by affinity electrophoresis.

Tryptophan residues and the sugar binding site of potato lectin.

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Potato lectin (Solanum tuberosum agglutinin, STA) was found to contain fluorescent tryptophan residues highly exposed to solvent. The binding of chitin oligosaccharides to STA induced fluorescence quenching, a shift of the fluorescence maximum to shorter wavelength, a decrease in the quenching
The creation of artificial metabolic sinks in plants by genetic engineering of key branch points may have serious consequences for the metabolic pathways being modified. The introduction into potato of a gene encoding tryptophan decarboxylase (TDC) isolated from Catharanthus roseus drastically
Potato plants (Solanum tuberosum cv. May Queen) transgenic for OASA1D, which encodes a point mutant of an alpha-subunit of rice (Oryza sativa) anthranilate synthase (AS, EC 4.1.3.27), were generated in order to determine the effects of the mutant gene on levels of free tryptophan (Trp) and AS

Fluorescence studies with potato carboxypeptidase inhibitor.

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Potato carboxypeptidase inhibitor (CPI) is a 39-residue globular protein whose X-ray structure is known. The protein's two tryptophan residues (W22 and W28) appear to be on the surface in the crystal structure. The fluorescence spectrum of CPI has a maximum at 344 nm. Acrylamide solute quenching

Effect of heat-induced aggregation on the IgE binding of patatin (Sol t 1) is dominated by other potato proteins.

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The interaction of the major potato allergen patatin, Sol t 1, with IgE was investigated on a quantitative level as a function of heat treatment at different temperatures. On the basis of a number of publications, potato is considered to be a heat-labile allergen, but the molecular explanation for

Circular dichroism and fluorescence studies on potato virus X and its structural components.

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Circular dichroism (DC) measurements of the coat protein subunits of potato virus X show that native subunits that can reassemble with RNA to form infectious virus particles have appreciable alpha-helical structure. The CD of intact potato virus X was less intense below and more intense above 250
The correlation between potato components and Maillard reaction derivative harmful products (MRDHPs) formation during heat-processing was assessed in nine commercial potato varieties in China. Principal component analysis (PCA) combined with canonical correlation analysis (CCA) approach was

The 42-kDa coat protein of Andean potato mottle virus acts as a transcriptional activator in yeast.

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Interactions of viral proteins play an important role in the virus life cycle, especially in capsid assembly. Andean potato mottle comovirus (APMoV) is a plant RNA virus with a virion formed by two coat proteins (CP42 and CP22). Both APMoV coat protein open reading frames were cloned into pGBT9 and
The objective of the study was to explore the formation mechanism and thermodynamic properties of chitosan (CS)-potato protein isolate (PPI) complex under DHPM treatment. The transmission electron microscopic (TEM) results showed the formation of a complex between CS and PPI. Meanwhile, particle
Plant parasitic nematodes are microscopic pathogens that invade plant roots and cause extensive damage to crops. We have used a chemical biology approach to define mechanisms underpinning their parasitic behaviour: We discovered that reserpine, a plant alkaloid that inhibits the vesicular monoamine

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

Differences in nucleotide-binding site of isoapyrases deduced from tryptophan fluorescence.

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Comparative studies of intrinsic and extrinsic fluorescence of apyrases purified from two potato tuber varieties (Pimpernel and Desirée) were performed to determine differences in the microenvironment of the nucleotide binding site. The dissociation constants (K(d)) of Pimpernel apyrase for the

Characterization of a Kunitz-type serine protease inhibitor from Solanum tuberosum having lectin activity.

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Plant lectins and protease inhibitors constitute a class of proteins which plays a crucial role in plant defense. In our continuing investigations on lectins from plants, we have isolated, purified and characterized a protein of about 20 kDa, named PotHg, showing hemagglutination activity from
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