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At least 163 records · Page 9Linked to original sources

PubMed1993

Variation of total hyoscine content of cultivated Datura metel Linn.

A titrimetric method is described for rapid assay of hyoscine content of organs of locally cultivated Datura metel Linn. Raw materials required (approximately 1.5 gm) are much less than those required for conventional percolation processes. Using the procedure, the flowers have been shown to be richest in hyoscine, only minimal levels of alkaloids being detected in the fruits. Furthermore, the total alkaloid content of D. metel has been shown to peak in the hot dry season, and at its lowest during the rainy season in Ibadan.

Agriculture↗

PubMed1994

Purification and characterization of O-acetylserine sulfhydrylase isoenzymes from Datura innoxia.

Three isoenzyme forms (designated A, B, and C) of O-acetylserine sulfhydrylase were purified from Datura innoxia suspension cultures. Isoenzyme A is the most abundant form, comprising 45-60% of the total activity. Isoenzymes C and B comprise 35-40% and 10-20% of the activity, respectively. The specific activities of the purified isoenzymes are similar (870-893 mumol of cysteine/min/mg of protein). Molecular masses for isoenzymes A, B, and C, estimated by analytical size exclusion high performance liquid chromatography, are 63, 86, and 63 kDa, respectively. Isoenzymes A and B are homodimers; isoenzyme C is a heterodimer. Spectral analysis indicates that these isoenzymes possess a pyridoxal 5'-phosphate cofactor that binds the O-acetylserine substrate. Binding is reversible by addition of the sulfide substrate. The O-acetylserine sulfhydrylase isoenzymes are active over a broad temperature range, with maximum activity between 42 and 58 degrees C. They are active only between pH 7 and 8, with optimal activity at pH 7.6. Kinetic analysis indicates these enzymes are allosterically regulated and exhibit positive cooperativity with respect to both substrates. They are inhibited by sulfide concentrations above 200 microM. The kinetic analysis together with the physical and spectrophotometric characteristics indicate that the O-acetylserine sulfhydrylase enzymes have two active sites.

Cells, Cultured↗

PubMed1996

Datura stramonium lectin staining of glial associated extracellular material in insect brains.

To investigate how glial cells structure the neuropile of olfactory pathways in the brains of honeybees and locusts, we used a lectin as a carbohydrate specific molecular label. On frozen sections, Datura stramonium lectin (DSL) stained extracellular material which is mainly associated with glial cells. Preadsorption of the DSL with the carbohydrate N, N'-diacetylchitobiose blocked the staining. The location of glial cells was detected by an antiserum against the glial-specific nuclear repo-protein. Lectin-staining surrounded the neuropile of the antennal lobe, axonal projections of olfactory relay neurons, and the mushroom body neuropile. Within the mushroom body neuropile of the bee, DSL-staining was especially intense at the branching sites of the Kenyon cell axons and in the ventral part of the alpha-lobe. The dissection of the various cellular contributions to the lectin-staining in dissociated cell cultures suggested that certain glial cells, but also neuronal somata of the antennal lobe and Kenyon cells of the mushroom bodies express the label. The expression of lectin-staining matures during the pupal development of the bee, whereas in larval stages of the hemimetabolous locust, the staining pattern appears already completed. Since carbohydrate recognition is thought to play an important role in the formation of neuronal networks, the glial derived extracellular material may contribute to the morphogenesis and structural integrity of the olfactory neuropiles.

Animals↗

PubMed2001

Determination of scopolamine, atropine and anisodamine in Flos daturae by capillary electrophoresis.

A capillary electrophoresis method was developed for the separation and determination of tropane alkaloids in Flos daturae plants. Separation was performed on a fused silica capillary(42.1 cm x 50 microm i.d.) at an applied voltage of 20 kV. Scopolamine, atropine and anisodamine were well separated in the buffer of 50 mmol/L phosphate buffer (pH 5.0) containing 20% (v/v) tetrahydrofuran (THF). Beer's law was obeyed in the range of concentration of 2.4-21.8 microg/mL for scopolamine, 4.0-36.0 microg/mL for atropine and 2.6-23.7 microg/mL for anisodamine, respectively, and the correlation coefficients were over 0.999 (n = 6). The developed method was applied for the analysis of herb samples.

Atropine↗

PubMed2006

Regionally specific distribution of the binding of anti-glutamine synthetase and anti-S100 antibodies and of Datura stramonium lectin in glial domains of the optic lobe of the giant prawn.

We previously characterized some crustacean glial cells by markers such as 2',3'-cyclic nucleotide 3'-phosphodiesterase and glial fibrillary acidic protein. Here we use antibodies against glutamine synthetase full-length molecule (anti-GS/FL), a GS C-terminal peptide (anti-GS/20aa-C), and brain S100 (anti-S100), as well as the binding of the insect glia and rat astrocytic marker Datura stramonium lectin (DSL), in the optic lobe of the prawn Macrobrachium rosenbergii. All markers label the lamina ganglionaris cartridge region (lighter: anti-GS/FL; heavier: DSL). In addition, anti-GS/FL labels superficial somata of external and internal medullas and internal chiasm cells. Both anti-GS/20aa-C and anti-S100 label heavily the glial sheaths of the lamina ganglionaris. In addition, anti-S100 binds to the perineurial glia of medullary parenchymal vessels. Western blot analyses show that both anti-GS/FL and anti-GS/20aa-C bind mostly to a band of 50-55 kDa, compatible with a long isoform of vertebrate GS, and accessorily to a possible dimer and, in the case of anti-GS/20aa-C, to an ill-defined band of intermediate mass. Binding of anti-S100 is selective for a single band of about 68 kDa but shows no protein in the weight range of the canonical S100 protein superfamily. DSL reveals two bands of about 75 and about 120 kDa, thus within the range of maximal recognition for rat astrocytes. Our results suggest that phenotype protein markers of the optic lobe glia share antigenic determinants with S100 and (a long form of) GS and that, similarly to vertebrate and insect glia, crustacean glia protein and N-glycan residue markers display regional heterogeneity.

Animals↗

PubMed1976

Particular small size RNA and RNA fragments from different origins as tumor inducing agents in Datura stramonium.

Particular RNA fragments obtained by action of pancreatic ribonuclease on purified RNAs originating from species totally unrelated to Agrobacterium tumefaciens (Escherichia coli, rabbit, monkey) are capable of inducing the formation of transplantable tumorous tissue when introduced at wounded sites in inverted stems of Datura stramonium maintained under axenic conditions on a medium containing auxin and kinetin. Reovirus RNA and a small size RNA (5-6S) isolated from RNA bound RNA directed DNA polymerase from Escherichia coli also induced the appearance of tumorous tissues which grow on solid synthetic medium in the absence of auxin and kinetin.

Animals↗

PubMed1989

Light and electron microscopic detection of (3 Gal beta 1,4 GlcNAc beta 1) sequences in asparagine-linked oligosaccharides with the Datura stramonium lectin.

The Datura stramonium lectin recognizes with high affinity the disaccharide N-acetyllactosamine (Gal beta 1,4 GlcNAc). We have developed a highly specific cytochemical affinity technique in which an ovomucoid-gold complex serves as second step reagent for the visualization of this lectin bound to reactive sequences present in tissue sections. The lectin binding sites were detected in semithin and ultrathin sections of aldehyde-fixed and low temperature Lowicryl K4M embedded tissues. For light microscopical labeling the photochemical silver reaction for signal amplification was required. The application of this technique for the detection of N-acetyllactosamine containing asparagine-linked oligosaccharides in various intracellular organelles and the plasma membrane is demonstrated.

Acetylgalactosamine↗

PubMed1986

Lectin binding studies on murine peritoneal cells: physicochemical characterization of the binding of lectins from Datura stramonium, Evonymus europaea, and Griffonia simplicifolia to murine peritoneal cells.

Purified 125I-labeled lectins from Datura stramonium, Evonymus europaea, and Griffonia simplicifolia (I-B4 isolectin) were used to analyze changes in the expression of carbohydrates on the surface of resident (PC) and thioglycollate-stimulated murine (C57B/6J) peritoneal exudate cells (PEC). The lectins from D. stramonium, E. europaea, and G. simplicifolia I-B4 bind specifically to PEC with relatively high affinity (Kd = 5.65 +/- 1.08 X 10(-7) M, 1.08 +/- 0.12 X 10(-8) M, and 1.33 +/- 0.15 X 10(-7) M, respectively). Assuming a single lectin molecule binds to each cell surface saccharide, the number of receptor sites per cell ranged for different cell samples from 22.3 to 50.0 X 10(6), from 3.8 to 4.8 X 10(6), and from 2.0 to 16.8 X 10(6) for D. stramonium, E. europaea, and G. simplicifolia I-B4 lectins, respectively. There were approximately 3- to 7-fold, 16- to 20-fold, and 2- to 20-fold increases in binding capacity for D. stramonium, E. europaea and G. simplicifolia I-B4, respectively, compared to the binding to resident, peritoneal cells. Scatchard plots of the binding of all three lectins to PEC were linear, suggesting that the receptor sites for these lectins are homogeneous and noninteracting. The binding capacity of these lectins to PEC was unchanged after trypsin digestion of cells. The expression of carbohydrates on the surface of PEC was also monitored by an agglutination assay. PEC were agglutinated by all three lectins whereas PC either were not agglutinated or were agglutinated only at high lectin concentrations. On the basis of our knowledge of the carbohydrate binding specificity of the D. stramonium and G. simplicifolia I-B4 lectins, we postulate that, parallel with thioglycolate stimulation, there is an increase in the number of N-acetyllactosamine residues and terminal alpha-D-galactosyl end groups. The blood group B, and H type 1 determinants--DGa1 alpha 1,3[LFuc alpha 1,2]DGa1 beta 1,3(or 4)DGlcNAc and LFuc alpha 1,2DGa1 beta 1,3DG1cNAc, respectively, as well as DGa1 alpha 1,3DGa1 beta 1,3(or 4)DGlcNAc--may be considered to be possible receptors for the E. europaea lectin. These glycoconjugates, present on the surface of peritoneal exudate cells, provide new chemical markers for studying the differentiation of resident peritoneal cells.

Agglutination Tests↗

PubMed1996

Benzalkonium chloride inhibited the histamine release from rat peritoneal mast cells induced by bradykinin and GlcNAc oligomer-specific lectin Datura stramonium agglutinin, but heparin did not.

1. Benzalkonium chloride (BAC) inhibited the histamine release from rat peritoneal mast cells induced by synthetic cationic polymers (compound 48/80 and PEI6), bradykinin, des-Arg1-bradykinin and des-Arg9-bradykinin and Datura stramonium agglutinin (DSA). 2. The anionic polymers heparin, de-N-sulfated heparin, poly-aspartic acid and poly-glutamic acid dose dependently inhibited the histamine release induced by cationic polymers, suggesting counteraction between anions and cations. 3. Inhibition by heparin was diminished but that of BAC remained after removal of extracellular heparin and BAC. 4. Mast cell activation by bradykinin and DSA was not inhibited by anionic polymers, suggesting that both bradykinin and DSA recognize membrane sites as receptors.

Animals↗

PubMed1995

Alkaloids of Datura ferox from Argentina.

Chromatographic procedures (HPLC, GC-MS) are outlined in this paper for the analysis of alkaloids in poisonous Datura ferox seeds of Argentina, from which previously only quantitative analysis for scopolamine was known. Five additional tropane alkaloids are now identified as 3 alpha-tigloyloxytropane (tigloyltropeine), 3-phenylacetoxy-6 beta,7 beta-epoxytropane (3-phenylacetoxyscopine), aposcopolamine (apohyoscine), 7 beta-hydroxy-6 beta-propenyloxy-3 alpha-tropoyloxytropane, traces of 7 beta-hydroxy-6 beta-isovaleroyloxy-3 alpha-tigloyloxytropane and a pyrrolidine alkaloid, hygrine. Two new structures, 3-phenylacetoxy-6 beta,7 beta-epoxytropane (3-phenylacetoxyscopine) and 7 beta-hydroxy-6 beta-propenyloxy-3 alpha-tropolyoxytropane, are proposed on the basis of their spectra. Hyoscyamine, nicotine and tropane N-oxides were not detected in all samples studied.

Alkaloids↗

PubMed1999

7-Hydroxywithanolides from datura ferox

Three new withanolides were isolated from leaves of Datura ferox. Their structures were established as (17R,20S,22R)-5alpha,6alpha, 7beta,12alpha-tetrahydroxy-1-oxowitha-2,24-dienolide (1), (17R,20S, 22R,24S,25S)-24,25-epoxy-5alpha,6alpha,7beta, 12alpha-tetrahydroxy-1-oxowitha-2-enolide (2), and (17R,20S, 22R)-5alpha,6alpha-epoxy-7alpha-hydroxy-1,12-dioxowitha-2, 24-dienolide (3), using spectroscopic methods (NMR, MS) and molecular modeling.

Journal Article↗

PubMed1975

Oxidase-peroxidase enzymes of Datura innoxia. Oxidation of reduced nicotinamide-adenine dinucleotide in the presence of formylphenylacetic acid ethyl ester.

The oxidase-peroxidase from Datura innoxia which catalyses the oxidation of formylphenylacetic acid ethyl ester to benzoylformic acid ethyl ester and formic acid was also found to catalyse the oxidation of NADH in the presence of Mn2+ and formylphenylacetic acid ethyl ester. NADH was not oxidized in the absence of formylphenylacetic acid ethyl ester, although formylphenylacetonitrile or phenylacetaldehyde could replace it in the reaction. The reaction appeared to be complex and for every mol of NADH oxidized 3-4 g-atoms of oxygen were utilized, with a concomitant formation of approx. 0.8 mol of H2O2, the latter being identified by the starch-iodide test and decomposition by catalase. Benzoylformic acid ethyl ester was also formed in the reaction, but in a nonlinear fashion, indicating a lag phase. In the absence of Mn2+, NADH oxidation was not only very low, but itself inhibited the formation of benzoylformic acid ethyl ester from formylphenylacetic acid ethyl ester. A reaction mechanism for the oxidation of NADH in the presence of formylphenylacetic acid ethyl ester is proposed.

Catalase↗

PubMed1996

Subcellular Location of O-Acetylserine Sulfhydrylase Isoenzymes in Cell Cultures and Plant Tissues of Datura innoxia Mill.

O-Acetylserine sulfhydrylase (OASS; EC 4.2.99.8) catalyzes the formation of L-cysteine from O-acetylserine and inorganic sulfide. Three OASS isoenzymes that differ in molecular mass and subunit structure are present in shoot and root tissues and in cadmium-resistant and cadmium-susceptible cell cultures of Datura innoxia Mill. Different OASS forms predominate in leaves, roots, and suspension-cell cultures. To determine the subcellular location of the OASS isoenzymes, purified mitochondria, chloroplasts, and cytosolic fractions from protoplasts were obtained. The isoenzymes are compartmentalized in D. innoxia cells, with a different isoenzyme predominant in the chloroplast, cytosol, and mitochondria, suggesting that they serve different functions in the plant cell. The chloroplast form is most abundant in green leaves and leaf protoplasts. The cytosolic form is most abundant in roots and cell cultures. A mitochondrial form is abundant in cell cultures, but is a minor form in leaves or roots. Cadmium-tolerant cell cultures contain 1.8 times as much constitutive OASS activity as the wild-type cell line, and 2.9 times more than the cadmium-hypersensitive cell line. This may facilitate rapid production of glutathione and metal-binding phytochelatins when these cultures are exposed to cadmium.

Journal Article↗

PubMed1980

A Nitrate Reductase-less Variant Isolated from Suspension Cultures of Datura innoxia (Mill.).

A comparative study has been carried out of the growth of two lines of Datura innoxia (Mill.) cells, designated DI-6 and NR1, their resistance to chlorate, and their ability to assimilate nitrate in sterile culture. The NR1 cell line was isolated from DI-6 cultures by first growing the latter in a nitrate-based medium for 5 days and then transferring the cells to a medium containing 2 grams liter(-1) of casein hydrolysate as the sole N source and 49 millimolar KClO(3) for a 6-week incubation period. Cells which survived the chlorate treatment then were transferred to casein hydrolysate medium and have been cultured in the absence of chlorate for more than 18 months (NR1).DI-6 cells can grow in a nitrate-based medium, whereas NR1 cells can take up nitrate but cannot use it as a N source. The inability of NR1 to assimilate nitrate appears to be due to the lack of an active nitrate reductase in these cells. Through the use of a variety of electron donors and acceptors, the lack of nitrate reductase activity in NR1 cells was shown to be due to the absence of, or a defect in, that component of the enzyme which mediates the reduction of nitrate to nitrite.In other experiments, DI-6 and NR1 were grown on a solid medium containing casein hydrolysate (2 grams liter(-1)) as the sole N source. Under these culture conditions, neither cell line contained an active nitrate reductase. The growth on this medium was compared to that on the same medium containing chlorate at concentrations from 0 to 100 millimolar. DI-6 culture growth was inhibited by 70% at a chlorate concentration of 30 micromolar, whereas growth of NR1 was stimulated by more than 60% on the same medium and by 100% at a chlorate concentration of 30 millimolar. In the presence of 100 millimolar chlorate, the growth of both cell lines was completely inhibited. This clear difference between the response of DI-6 and NR1 cells to chlorate even in the absence of nitrate lends support to the observations by others that chlorate inhibits cells by a mechanism other than, or in addition to, its nitrate reductase-catalyzed conversion to chlorite.Nitrite reductase was induced by nitrate in NR1 cells as well as in DI-6. This observation is a further confirmation of the fact that nitrate, not nitrite, is the true inducer of the nitrate assimilatory pathway in higher plants.

Journal Article↗

PubMed1983

Expression of 5-Methyltryptophan Resistance in Plants Regenerated from Resistant Cell Lines of Datura innoxia.

Seventy-nine 5-methyltryptophan-resistant cell lines have been selected from haploid Datura innoxia Mill. cell cultures by plating suspensions in agar medium containing a growth inhibitory concentration of 5-methyltryptophan. Mutagen treatment increased the frequency of resistance. The eleven variants tested posses an altered anthranilate synthase less sensitive to feedback inhibition by tryptophan. All five of the variants which were analyzed for free amino acids contained elevated levels of free tryptophan (8 to 30 times the wild type level). None of the selected cell lines were auxin-autotrophic. Resistance to 5-methyltryptophan, altered anthranilate synthase, and high free tryptophan (4 to 44 times) were also expressed in leaves of plants regenerated from the variant lines and in cultures reinitiated from the resistant plants. These results show that the amino acid overproduction phenotype can be selected at the cellular level of organization and be expressed identically in whole plants regenerated from the selected cells.

Journal Article↗

PubMed1983

Mass spectrometric analysis of cytokinins in plant tissues : v. Identification of the cytokinin complex of datura innoxia crown gall tissue.

The cytokinin complex of Datura innoxia Mill. crown gall tissue was purified by ion exchange, Sephadex LH-20 chromatography and reversed-phase high performance liquid chromatography. By gas chromatography-mass spectrometry using (2)H-labeled compounds, the following cytokinins were identified in the basic fraction eluting from a cation exchange column: zeatin, zeatin riboside, dihydrozeatin, dihydrozeatin riboside, their corresponding O-glucosides, 7- and 9-glucosides of zeatin, 9-glucoside of dihydrozeatin, isopentenyladenine, and isopentenyladenosine. Zeatin riboside 5'-monophosphate was the major cytokinin nucleotide in the tissue. In addition, dihydrozeatin riboside and isopentenyladenosine were identified in the nucleotide fraction following enymic degradation.

Journal Article↗

PubMed1984

Selection, Isolation, and Characterization of Cadmium-Resistant Datura innoxia Suspension Cultures.

Datura innoxia cells from suspension cultures were selected for their ability to grow and divide rapidly in normally lethal concentrations of cadmium. Cells resistant to 12.5, 25, 50, 100, 160, 200, and 250 micromolar cadmium chloride were isolated and utilized to initiate cell suspension cultures resistant to this toxic metal ion. Variant cell lines retained their ability to grow in cadmium after being grown in its absence for more than 400 generations. Resistance to cadmium was correlated with the synthesis of low molecular weight, cysteine-rich, cadium-binding proteins. Synthesis of these proteins was induced rapidly in cadmium-resistant cells in response to a challenge of cadmium. Induction was detectable within one hour after exposure of the cells to the metal ion. Accumulation of protein bound cadmium reached a maximum eight to twelve hours following exposure. Metal-binding proteins were not detectable in the cadmium sensitive D. innoxia cells from which resistant cells were derived.

Journal Article↗

PubMed1987

Determination by Gas Chromatography-Mass Spectrometry of [N(5)]Adenine Incorporation into Endogenous Cytokinins and the Effect of Tissue Age on Cytokinin Biosynthesis in Datura innoxia Crown Gall Tissue.

In this study gas chromatographic-mass spectrometric techniques have been used to identify and quantify the metabolic incorporation of [(15)N(5)]adenine into zeatin and its metabolites by 3-week-old Datura innoxia Mill, crown gall tissue. In a parallel study the levels of endogenous cytokinins were also determined by the stable isotope dilution technique using deuterium ((2)H)-labeled internal standards. Incorporation levels of the [(15)N(5)]adenine after 8 hours of incubation, expressed as a percentage of the endogenous cytokinins, were as follows: zeatin (1.0%), zeatin riboside (1.5%), and zeatin riboside 5'-phosphate (10.2%). These results are consistent with those observed in complementary experiments using [U-(14)C]adenine, and support the proposal that the cytokinin biosynthesis occurs primarily at the nucleotide level. The effect of tissue age on cytokinin biosynthesis, determined by [U-(14)C]adenine incorporation into cytokinins by tissues at varying growth stages, indicated a steady increase with time reaching maximal synthesis at five weeks following subculture after which the level of (14)C incorporation into cytokinins declined.

Journal Article↗