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canavalia ensiformis/アルブミン

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[Electrophoretic study of albumins and globulins of 4 genotypes of Canavalia ensiformis].

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Polyacrylamide gel electrophoresis (PAGE) and PAGE-SDS were used to study seed albumins and globulins of Canavalia ensiformis. In PAGE the concentration of acrylamide used in the upper gel was 4.0% with a pH of 6.7 and in the lower gel 7.5% and 10% of acrylamide were used with a pH of 8.9. In

Natural plant enzyme inhibitors: isolation and properties of a trypsin inhibitor from jack bean (Canavalia ensiformis).

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A protease inhibitor which is equally active on bovine and porcine trypsins was isolated in a homogenous form from jack bean (Canavalia ensiformis). The preparation with a molecular weight of 18 kDa was found to be a glycoprotein with a high half cysteine content. Isoleucine and tyrosine were found

Localization of lectin-binding sites and sugar-binding proteins in tachyzoites of Toxoplasma gondii.

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Lectins and neoglycoproteins labeled with colloidal gold particles were used for the ultrastructural localization of carbohydrate residues and sugar-binding sites, respectively, in thin sections of tachyzoites of Toxoplasma gondii embedded in the Lowicryl K4M resin. Incubation of the sections in the
In India, the seeds of Canavalia gladiata and C. ensiformis have traditionally been eaten by the aborigines, but they are less popular among the civilized people. The data on the chemical composition and nutritional quality of these seeds are not readily available. The proximate composition, mineral

Studies on lectins. XL. O-glycosyl derivatives of Spheron in affinity chromatography of lectins.

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Free monosaccharides can be used for direct glycosylation of Spheron, a spherical macroporous hydroxyalkyl methacrylate-ethylene dimethacrylate copolymer, in a reaction that proceeds at room temperature in dioxane medium under catalysis of dry HCl or BF3. Derivatives of L-fucose, D-galactose,

Purification and properties of alpha-D-mannosidase from jack-bean meal.

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1. alpha-Mannosidase from jack-bean meal was purified 150-fold. beta-N-Acetyl-glucosaminidase and beta-galactosidase were removed from the preparation by treatment with pyridine. Zn(2+) was added during the purification to stabilize the alpha-mannosidase. 2. At pH values below neutrality,

Electron microscopic visualization by the unlabelled lectin/antiferritin-antibody/ferritin method of lectin receptors on cell surfaces.

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For electron microscopic demonstration of carbohydrate moieties on cell surfaces of HeLa-cells the lectins from Viscum albumin, Canavalia ensiformis and Dolichos biflorus have been used. The staining experiments were performed by reaction of the cell surface receptor localized lectin with purified

Preparation and evaluation of lactose-modified monoliths for the adsorption and decontamination of plant toxins and lectins.

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A series of sugar-modified porous silica monoliths with different sugar ligands (β-lactoside, β-N-acetyllactosaminide, β-d-galactoside, β-d-N-acetylgalactosaminide and β-d-glucoside) and linkers were prepared and evaluated using plant toxins and lectins including ricin and a Ricinus communis

Purification of urease from Ureaplasma urealyticum.

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We have purified urease from the Mollicutes, Ureaplasma urealyticum, using high performance liquid chromatography methods and DEAE-Sephadex chromatography. While only small amounts of material could be utilized in these methods, urease was purified at least 180-fold, yield a major band on SDS-PAGE

The activation of urease.

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1. It has been shown that the activity of solutions of twice recrystallized urease is reversibly increased by moderate heating and reversibly decreased by storage in the cold, even in the frozen state. 2. Crude extracts of jack bean meal containing potent urease undergo this same type of reversible

Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology.

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Extracts of leaves, seeds, roots, and stem from a tropical legume, C. ensiformis, were prepared employing buffers and detergent in aqueous solution. Leaf extracts had the highest protein content and the most pronounced peptidase activity with optimal pH in the neutral to alkaline range. All extracts

Cross-linked enzyme lyophilisates (CLELs) of urease: A new method to immobilize ureases.

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In this study, we presented a new approach for immobilizing JBU (Jack bean urease), by producing urease cross-linked enzyme lyophilisates (CLELs). Through the use of bovine serum albumin (BSA), lyophilisation, cross-linking with dextran polyaldehyde (DPA), and optimizing cross-linker pH, the

[Characteristics of Canavalia proteins].

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The purpose of this work was the isolation and characterization of grain protein from five Venezuelan Genotypes (U-02, Yaracuy, Valle De La Pascua, Originally Tovar) of Jack Bean (Canavalia ensiformis). The average protein content from these genotypes was 31.37%, it ranged between 28.44% and 33.05%.
The experiment was carried out to investigate the inclusion of underutilised legumes, Entada scandens, Canavalia gladiata and Canavalia ensiformis, seed meal in soybean-based diet in broilers. The utilisation of these wild legumes is limited by the presence of antinutrient compounds. Processing

Breakdown of gastric mucus in presence of Helicobacter pylori.

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The potential of Helicobacter pylori to degrade gastric mucus was examined. Colonies of H pylori cultured from antral mucosal biopsy specimens of patients with non-autoimmune gastritis were washed with sterile saline, passed through a sterilisation filter, and the filtrate examined for urease,
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