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phaseolus/carbohydrate
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Growth, photosynthesis and storage of carbohydrates and nitrogen in Phaseolus lunatus in relation to resource availability.
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Growth, photosynthesis, and storage of nitrogen (N) and total non-structural carbohydrates (TNC) of a perennial wild type and an annual cultivar of lima bean (Phaseolus lunatus) were examined at different light intensities and N supplies. Relative growth rate and photosynthesis increased with light
Blocking carbohydrate absorption and weight loss: a clinical trial using Phase 2 brand proprietary fractionated white bean extract.
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BACKGROUND
Phase 2' starch neutralizer brand bean extract product ("Phase 2") is a water-extract of a common white bean (Phaseolus vulgaris) that has been shown in vitro to inhibit the digestive enzyme alpha-amylase. Inhibiting this enzyme may prevent the digestion of complex carbohydrates, thus
A method for (13)C-labeling of metabolic carbohydrates within French bean leaves (Phaseolus vulgaris L.) for decomposition studies in soils.
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The molecular composition of plant residues is suspected to largely govern the fate of their constitutive carbon (C) in soils. Labile compounds, such as metabolic carbohydrates, are affected differently from recalcitrant and structural compounds by soil-C stabilisation mechanisms. Producing
[CARBOHYDRATE METABOLISM IN TYPE 1 DIABETIC RATS UNDER THE CONDITIONS OF THE KIDNEY BEAN PODS AQUEOUS EXTRACT APPLICATION].
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The influence of the aqueous pods extract of kidney bean (Phaseolus vulgaris) on indicators of carbohydrate metabolism under the condition of experimental type 1 diabetes in rats was studied. It was shown that long-term oral administration of the extract at a dose of 200 mg/kg to rats leads to the
Potential efficacy of preparations derived from Phaseolus vulgaris in the control of appetite, energy intake, and carbohydrate metabolism.
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Preclinical data on extracts of and preparations derived from beans of Phaseolus vulgaris are reviewed as potential remedies for use in controlling food consumption, body weight, lipid accumulation, and glycemia. A growing body of evidence suggests that acute and chronic administration of P.
The Isolation of Carbohydrate-binding Peptide from Scarlet Runner Bean Lectin.
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The carbohydrate-binding peptide fragment of scarlet runner bean (Phaseolus coccineus var. rubronanus) lectin has been prepared by trypsin digestion. The carbohydrate-binding peptide was isolated from digested solution by affinity chromatography on thyroglobulin-Sepharose column, Bio-Gel P-4 gel
Compartmentation of soluble carbohydrates, of starch and of malate in motor organs (pulvini) and other parts of Phaseolus coccineus L. leaves.
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Quantitative histochemistry was used to investigate the tissue-specific compartmentation of soluble carbohydrates (sucrose, glucose, fructose), starch and malate in the laminar pulvinus, leaf blade and petiole of Phaselous coccineus L. at day and night positions of diurnal leaf movement. Total
Isolation from lima bean lectin of a peptide containing a cysteine residue essential for carbohydrate binding activity.
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The location and amino acid sequence surrounding a cysteine residue required for carbohydrate binding in the lima bean lectin (LBL) was determined. Following selective conversion of the sulfhydryl group to its S-cyano derivative, LBL was cleaved at the essential cysteine residue to give two
Fluorescence energy transfer studies on lima bean lectin. Distance between the subunit hydrophobic binding site and the thiol group essential for carbohydrate binding.
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Measurements of the efficiency of singlet-singlet energy transfer were used to determine the distance between the hydrophobic binding site and the thiol group required for carbohydrate-binding activity of lima bean lectin. 1-Anilino-8-naphthalenesulfonate, bound to the hydrophobic binding site by
Site-directed mutagenesis studies on the lima bean lectin. Altered carbohydrate-binding specificities result from single amino acid substitutions.
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The wild-type seed lima bean lectin (LBL), and recombinant LBL expressed in Escherichia coli show specificity for the human blood group A immunodominant trisaccharide GalNAc alpha 1-3[Fuc alpha 1-2]Gal beta 1-R. We have generated four site-specific mutants of LBL, two of which show altered
Giardia cyst wall-specific carbohydrate: evidence for the presence of galactosamine.
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Gas chromatographic (GC), mass spectrometric (MS), lectin binding and enzymatic analyses of the carbohydrates from Giardia cyst walls, intact cysts and trophozoites were performed to investigate the carbohydrate composition of Giardia cyst walls and to test the hypothesis that the Giardia cyst wall
Surface carbohydrate changes on Onchocerca lienalis larvae as they develop from microfilariae to the infective third-stage in Simulium ornatum.
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Use was made of seven FITC labelled lectins as tools to investigate the surface of Onchocerca lienalis larvae as they develop through to the infective third-stage in a natural vector, Simulium ornatum. The lectins were derived from Canavalia ensiformis (Con A), Lens culinaris (lentil), Triticum
Carbohydrates in the cell surface of hair cells from the guinea pig cochlea.
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The presence of cell surface carbohydrates was investigated in intact, non-fixed outer hair cells (OHCs) of guinea pigs using fluorescein isothiocyanate (FITC) and rhodamine (TRITC) lectins. By means of wheat germ agglutinin (WGA) N-acetyl-D-glucosamine was shown in the entire OHC membrane,
A rat bioassay for measuring the comparative availability of carbohydrates and its application to legume foods, pure carbohydrates and polyols.
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An assay was developed to evaluate the bioavailability of dietary carbohydrate by slope-ratio analysis of weight gain and plasma ketones of rats fed a carbohydrate-free diet supplemented with glucose as a standard and selected food items, pure carbohydrates and polyols. The diet was based on 35%
Identification of N-acetylgalactosamine in carbohydrates of Xenopus laevis testis.
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Identification of glycans in amphibian testis has shown the existence of N-acetylgalactosamine (GalNAc)-containing carbohydrates. Labeling of the sperm acrosome with GalNAc-binding lectins has allowed the identification of GalNAc-containing glycans in this organelle. Futhermore, this specific
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