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potato/phosphatase
Povezava se shrani v odložišče
Stran 1 iz 271 rezultatov
Superactivity and phase-sensitivity of potato acid phosphatase entrapped in reverse micelles.
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Prijava / prijava
Potato acid phosphatase, AcPase (E.C. 3.1.3.2) was entrapped in reverse micelles of cationic surfactant cetyltrimethylammonium bromide (CTAB) in isooctane and chloroform (1:1). The activity was studied at different values of Wo = ([water]/[surfactant]). AcPase exhibited superactivity in the reverse
Ingestion of potato starch containing esterified phosphorus increases alkaline phosphatase activity in the small intestine in rats.
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Alkaline phosphatase (ALP) hydrolyzes a variety of monophosphate esters and plays an important role in phosphorus (P) metabolism. Several nutrients in food have been reported to affect intestinal ALP activity in animal models. Previous reports indicated that high levels of P or phosphate in diets
Age- and diapause-related acid and alkaline phosphatase activities in the intestine and malpighian tubules of the Colorado potato beetle, Leptinotarsa decemlineata (Say).
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Specific activities for soluble (s) and membrane (m)-bound acid (ACP) and alkaline phosphatases (ALP) were determined in the midgut, hindgut, and Malpighian tubules for developing, prediapausing, and diapausing adult Colorado potato beetles, Leptinotarsa decemlineata (Say). High ACP activities were
Stability and activity of potato acid phosphatase in aqueous surfactant media.
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The effect of three different classes of surfactants viz., anionic, cationic and neutral on catalytic activity of potato acid phosphatase (AcPase) was studied. Anionic surfactants bis(2-ethylhexyl) sodium sulfosuccinate (AOT) and sodium dodecyl sulfate (SDS) inhibited AcPase activity completely at 3
A scFv-alkaline phosphatase fusion protein which detects potato leafroll luteovirus in plant extracts by ELISA.
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A single chain Fv antibody fragment (scFv) was obtained from a synthetic phage-antibody library after four rounds of selection against purified preparations of potato leafroll luteovirus (PLRV). Nucleotide sequence analysis showed that the scFv belongs to the human V(H)3 family. DNA encoding the
Enhancement of lateral flow immunoassay by alkaline phosphatase: a simple and highly sensitive test for potato virus X.
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Alkaline phosphatase (ALP) was used as an amplification tool in lateral flow immunoassay (LFIA). Potato virus Х (PVX) was selected as a target analyte because of its high economic importance. Two conjugates of gold nanoparticles were applied, one with mouse monoclonal antibody against PVX and one
Sucrose increases calcium-dependent protein kinase and phosphatase activities in potato plants.
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The effect of sucrose on tuber formation, calcium-dependent protein kinase (CDPK) and phosphatase activities was analysed using in vitro cultured potato plants. In short treatments, sucrose induced CDPK and phosphatase activities. In long treatments, sucrose induced tuber formation in the absence of
Immunogenic properties of rapidly digested food proteins following gavage exposure of mice: a comparison of ovalbumin with a potato acid phosphatase preparation.
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The ability of food proteins to resist digestion in simulated gastric fluid (SGF) correlates with allergenic potential. The purpose of the current investigations was to determine whether this association is due solely to the failure of unstable proteins to elicit an immune response when administered
A purple acid phosphatase from sweet potato contains an antiferromagnetically coupled binuclear Fe-Mn center.
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A purple acid phosphatase from sweet potato is the first reported example of a protein containing an enzymatically active binuclear Fe-Mn center. Multifield saturation magnetization data over a temperature range of 2 to 200 K indicates that this center is strongly antiferromagnetically coupled.
Purification and characterization of purple acid phosphatase PAP1 from dry powder of sweet potato.
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Purple acid phosphatase (PAP) was purified from sweet potato dry powder, which is used as a food additive. Spectrometric and enzymatic analyses, and analysis of the amino-terminal sequence indicated that the purified purple acid phosphatase was PAP1. High activity in neutral and acidic conditions,
Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase.
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Purple acid phosphatases (PAPs) are a family of binuclear metalloenzymes that catalyze the hydrolysis of phosphoric acid esters and anhydrides. A PAP in sweet potato has a unique, strongly antiferromagnetically coupled Fe(III)-Mn(II) center and is distinguished from other PAPs by its increased
Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato.
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Purple acid phosphatase from sweet potato is a homodimer of 110 kDa. Two forms of the enzyme have been characterized. One contains an Fe-Zn centre similar to that previously reported for red kidney bean purple acid phosphatase. Another isoform, the subject of this work, is the first confirmed
Sweet potato acid phosphatase immobilized on glutaraldehyde-activated aminopropyl controlled-pore glass: activation, repeated use and enzyme fatigue.
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Sweet potato acid phosphatase was covalently coupled with glutaraldehyde to aminopropyl controlled-pore glass, and used as a pre-column enzyme reactor. The immobilized enzyme reactor (IMER) was continuously operated using an automated chromatographic detection system we developed. Functional
A pathogen-responsive cDNA from potato encodes a protein with homology to a phosphate starvation-induced phosphatase.
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Infiltration of potato leaves with the phytopathogenic bacteria Pseudomonas syringae pv. maculicola induces local and systemic defense gene expression as well as increased resistance against subsequent pathogen attacks. By cDNA-AFLP a gene was identified that is activated locally in potato leaves in
Acid phosphatase of potato tubers (Solanum tuberosum L). Purification, properties, sugar and amino acid composition.
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1. Acid phosphatase (AcPase) from potato tubers was purified by tannic acid fractionation, DEAE-cellulose chromatography, filtration on Bio-Gel P-150 and affinity chromatography on Con A-Sepharose. The enzyme was purified 260-fold and was electrophoretically homogeneous; its mol. mass is about 69
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