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potato/protease

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ArticoleStudii cliniceBrevete
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Cytotoxic effect of potato aspartic proteases (StAPs) on Jurkat T cells.

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StAPs are potato aspartic proteases with cytotoxic activity against plant pathogens and spermatozoa. StAPs cytotoxic activity is selective, since these proteins do not exert toxic effect on plant cells and erythrocytes. In this work, we investigated the capacity of StAPs to exert cytotoxicity on

Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serine protease inhibitor from potato.

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Potato serine protease inhibitor (PSPI) constitutes about 22% of the total amount of proteins in potato tubers (cv. Elkana), making it the most abundant protease inhibitor in the plant. PSPI is a heterodimeric double-headed Kunitz-type serine protease inhibitor that can tightly and simultaneously

A cysteine protease gene is expressed early in resistant potato interactions with Phytophthora infestans.

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A potato cysteine protease (cyp) cDNA expressed at an early stage of an incompatible interaction with Phytophthora infestans was isolated. Both the nucleotide and deduced amino acid sequences are highly homologous to those of a tomato cysteine protease, CYP1. Striking protein similarity to all known

Separation of patatins and protease inhibitors from potato fruit juice with clay minerals as cation exchangers.

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Potato fruit juice as a by-product of the starch industry contains proteins with interesting functionalities such as protease inhibitors or patatin with its high nutritional value. Due to their functional properties, these proteins are principally of industrial interest. A drawback for the

Light scattering determination of the stoichiometry for protease-potato serine protease inhibitor complexes.

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The interaction between pancreatic proteases and a serine protease inhibitor purified from potato tubers was investigated by chromatography-coupled light scattering measurements. The molar mass distribution in the chromatogram was compared to theoretical values calculated for the different possible

Protease inhibitor from insect silk-activities of derivatives expressed in vitro and in transgenic potato.

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Several recombinant derivatives of serine protease inhibitor called silk protease inhibitor 2 (SPI2), which is a silk component in Galleria mellonella (Lepidoptera, Insecta), were prepared in the expression vector Pichia pastoris. Both the native and the recombinant protease inhibitors were highly

Enzymatic generation of peptides from potato proteins by selected proteases and characterization of their structural properties.

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The use of low grade starting material for the generation of peptides with bioactivity properties is of interest. The proteins from the potato starch industry byproduct is a promising source, as several health benefits may be associated with their hydrolysates. The efficiency of selected proteases

The action of potato inhibitors on activation of zymogen forms of digestive system proteases.

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The potato inhibitors of proteases inhibit the activation of trypsinogen, chymotrypsinogen, proelastase, procarboxypeptidase A and B induced by trypsin. These inhibitors do not inhibit the activation of trypsinogen induced by enterokinase. Potato inhibitors have no influence on pepsinogen

Conformational stability of the potato serine protease inhibitor group.

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The thermal unfolding of potato serine protease inhibitor (PSPI), the most abundant protease inhibitor group in potato tuber, was measured using far UV CD spectroscopy, fluorescence spectroscopy, and DSC. The results indicate that the thermal as well as the guanidinium-induced unfolding of PSPI

Synergistic antifibrinolytic action of the potato protease inhibitor and epsilon-aminocaproic acid.

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Fibrinolysis inhibition by a mixture of potato inhibitor and E-aminocaproic acid was greater than might be expected from the sum of the antifibrinolytic effects of these inhibitors investigated separately. This inhibition was observed in studies on the plasma euglobulin fraction and in a system
In this study, the RT-PCR method was used to detect the Y virus in potato tubers and leaves. Samples suspicious of virus infection with symptoms of virus infection were gathered from farms in Kermanshah and placed in plastic bags and kept at -80 degrees C temperature in order to maintain the RNA of
Potato aspartic proteases (StAPs) and their swaposin domain (StAsp-PSI) are proteins with cytotoxic activity which involves plasma membrane destabilization. The ability of these proteins to produce cell death varies with the cellular type. Therefore, StAPs and StAsp-PSI selective cytotoxicity could
Ultrastructural changes to the midgut epithelium of nymphs of the black field cricket (Teleogryllus commodus) after ingestion of potato protease inhibitor II (PPI-II) (0.6% (w/v) in artificial diet) were determined by light and electron microscopy. Crickets fed diet containing PPI-II grew more

Potato protease inhibitors inhibit food intake and increase circulating cholecystokinin levels by a trypsin-dependent mechanism.

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OBJECTIVE To investigate the mechanisms underlying the satiety-promoting effects of a novel protease inhibitor concentrate derived from potato (PPIC). METHODS The acute and prolonged effects of oral PPIC administration (100 mg kg(-1) per day) on food intake, body weight and gastric emptying were
To examine the proteolytic activities of various truncated derivatives of the potato virus Y (PVY) 50-kDa protease, the derivatives were expressed in Escherichia coli in polyprotein forms fused with coat protein (CP). For the intermolecular cleavage reaction, the truncated proteases were expressed
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