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At least 19 recordsLinked to original sources
PubMed2001

Samsonia erythrinae gen. nov., sp. nov., isolated from bark necrotic lesions of Erythrina sp., and discrimination of plant-pathogenic Enterobacteriaceae by phenotypic features.

Bacterial strains isolated from diseased erythrina (Erythrina sp.) trees in Martinique (French West Indies) were studied using phenotypic tests, 16S rDNA sequence analysis and DNA-DNA hybridization. Numerical analysis of phenotypic characteristics showed that these strains formed an homogeneous phenon among plant-pathogenic Enterobacteriaceae, and gave useful and updated information for the identification of these bacteria. Results of DNA-DNA hybridization indicated that strains from erythrina belonged to a discrete genomospecies (89-100% hybridization) and had low levels of DNA relatedness (2-33% hybridization) with reference strains of phytopathogenic Erwinia, Brenneria, Pectobacterium, Pantoea and Enterobacter species. 16S rDNA sequence analysis using three different methods revealed that the position of strain CFBP 5236T isolated from erythrina was variable in the different trees, so that strains from erythrina could not be assigned to any recognized genus. It is proposed that these strains are included in a new genus, Samsonia. The name Samsonia erythrinae is proposed for the new species. The G+C content of the DNA of the type strain, CFBP 5236T (= ICMP 13937T), is 57.0 mol%.

Base Composition↗
PubMed1999

Biosynthesis of Erythrina alkaloids in Erythrina crista-galli.

A precursor application system was developed to allow the study of Erythrina alkaloid formation in Erythrina crista-galli. Fruit wall tissue of this species was recognized as the major site of alkaloid biosynthesis. The application of radioactively and 13C-labelled potential precursors showed that the hitherto assumed precursor (S)-norprotosinomenine was not incorporated into the Erythrina alkaloids. In contrast, (S)-coclaurine as well as (S)-norreticuline were metabolized to erythraline and erythrinine, respectively, suggesting that a coclaurine-norreticuline pathway is operative in Erythrina alkaloid formation. Feeding of [1-13C]-labelled (S)-norreticuline with subsequent NMR spectroscopy demonstrated that the resulting erythraline was exclusively labelled at position C-10. Therefore, the participation of a symmetrical intermediate of the diphenoquinone type in Erythrina alkaloid biosynthesis can be excluded.

Alkaloids↗
PubMed2006

Application of an enzyme-linked immunosorbent assay for the analysis of imidacloprid in wiliwili tree, Erythrina sandwicensis O. Deg, for control of the wasp Quadrastichus erythrinae.

A monoclonal antibody-based enzyme-linked immunosorbent assay (ELISA) for the neonicotinoid insecticide imidacloprid was evaluated for its reproducibility, accuracy, and comparability to results from a conventional high-performance liquid chromatography (HPLC) for the analysis of imidacloprid in the endemic wiliwili tree (Erythrina sandwicensis O. Deg) found in dryland forests and landscapes in Hawaii. Imidacloprid was applied to these wiliwili trees in an attempt to control the newly introduced erythrina gall wasp, Quadrastichus erythrinae Kim. Leaf samples were freeze-dried and extracted with acidic aqueous methanol followed by methylene chloride partitioning. After solvent removal, the extract residue was reconstituted in 1 mL of water/methanol (1:1, v/v) for ELISA; no significant matrix interference was observed at 10-fold or more dilution. The average recoveries of imidacloprid from fortified samples ranged from 78% to 100% by ELISA. The correlation between the ELISA and HPLC results was excellent (r2 = 0.98). Imidacloprid was detected with the ELISA in all treated samples and its level varied in the samples among different treatments and in those from different parts of the trees. The infestation severity rating of leaf samples was inversely related to the concentration of imidacloprid. It is clear that imidacloprid effectively controls the wasps. The ELISA is a suitable method for quantitative and reliable determination of imidacloprid in wiliwili trees and the application provides information to understand how to control the wasps.

Chromatography, High Pressure Liquid↗
PubMed1994

Characterization of binding of Gal beta 4GlcNAc-specific lectins from Erythrina cristagalli and Erythrina corallodendron to glycosphinogolipids. Detection, isolation, and characterization of a novel glycosphinglipid of bovine buttermilk.

The lectins from seeds of Erythrina cristagalli and Erythrina corallodendron were characterized for binding to glycolipids, using a chromatogram binding assay, a microtiter well assay, and glycolipids coated on erythrocytes. Both lectins bound to glycolipids having a terminal Gal beta 4GlcNAc sequence and also, with similar affinity, to glycolipids with terminal Fuc alpha 2Gal beta 4GlcNAc (blood group H determinant on a type 2 chain). All other substitutions of Gal beta 4GlcNAc tested abolished the binding. A binding epitope for the Erythrina lectins was considered by comparison of minimum energy conformations of binding and nonbinding glycolipids. A non-acid glycolipid, with lectin binding activity, was found in bovine buttermilk. By mass spectrometry and proton NMR spectroscopy it was shown to be a branched hexaglycosylceramide with the structure Gal beta 4Glc-NAc beta 6(Gal beta 4GlcNAc beta 3)Gal beta 4Glc beta Cer. This glycosphingolipid has not been reported before.

Animals↗
PubMed2004

Central activity of hydroalcoholic extracts from Erythrina velutina and Erythrina mulungu in mice.

This work studied the central behavioural effects of hydroalcoholic extracts from the stem bark of Erythrina velutina and Erythrina mulungu on the elevated plus maze, open field, and rota rod tests in mice. These medicinal plants belong to the Fabaceae family and are popularly used in Brazil for their effects on the central nervous system. Single doses of the extracts were administered orally (200, 400 or 800 mg kg(-1)) or intraperitoneally (200 or 400 mg kg(-1)) to female mice. A reduction of the locomotor activity was observed in the open field test with both hydroalcoholic extracts after intraperitoneal treatment with all doses, but only with the highest dose after oral administration. In addition, oral and intraperitoneal administration of the extracts decreased the incidence of rearing and grooming. Decreases in the number of entries in the open (NEOA) and closed (NECA) arms of the elevated plus maze were observed after the administration of the highest dose (800 mg kg(-1), p.o.) of both hydroalcoholic extracts, and this effect may be due to the decrease in locomotor activity. These hydroalcoholic extracts failed to affect the motor coordination in the rota rod test. In conclusion, we showed that the hydroalcoholic extracts of E. velutina and E. mulungu have depressant effects on the central nervous system, which, at least partially, corroborates the popular use of these species as tranquilizers in Brazilian popular medicine.

Administration, Oral↗
PubMed2003

Antinociceptive activities of the hydroalcoholic extracts from Erythrina velutina and Erythrina mulungu in mice.

This work studied the antinociceptive effects of the hydroalcoholic extracts (HAEs) from Erythrina velutina (Ev) and Erythrina mulungu (Em) in three experimental models of nociception in mice. The extract was administered intraperitoneally to female mice at the doses of 200 and 400 mg/kg. Inhibitions of abdominal contractions were observed with the doses of 200 (88.6%; 86.8%) and 400 (95.5%; 83.5%) mg/kg of E. velutina and E. mulungu, respectively, as compared to controls. E. velutina and E. mulungu, at both doses, reduced the nociception produced by formalin in the 1st and 2nd phases and this effect was not reversed by the pretreatment with naloxone. In the hot plate test an increase of the reaction time was observed only at 60 (Ev=18.0+/-2.2; Em=20.8+/-2.52) and 90 min (Ev=20.4+/-1.71; Em=23.7+/-2.32) after the treatment with E. velutina and E. mulungu at the dose of 400 mg/kg as compared to controls (T60=11.1+/-0.74; T90=11.9+/-0.86). This effect was not reversed by naloxone. We conclude that E. velutina and E. mulungu presents antinociceptive effects, which are independent of the opioid system.

Analgesics↗
PubMed2006

Effect of Erythrina velutina and Erythrina mulungu in rats submitted to animal models of anxiety and depression.

Erythrina velutina (EV) and Erythrina mulungu (EM), popularly used in Brazil as tranquilizing agents, were studied. The effects of acute and chronic oral treatment with a water:alcohol extract of EV (7:3, plant grounded stem bark; acute = 100, 200, 400 mg/kg; chronic = 50, 100, 200 mg/kg) were evaluated in rats (N = 11-12) submitted to the elevated T-maze (for avoidance and escape measurements) model of anxiety. This model was selected for its presumed capacity to elicit specific subtypes of anxiety disorders recognized in clinical practice: avoidance has been related to generalized anxiety and escape to panic. Additionally, animals were treated with the same doses of EV and EM (water:alcohol 7:3, inflorescence extract) and submitted to the forced swim test for the evaluation of antidepressant activity (N = 7-10). Both treatment regimens with EV impaired elevated T-maze avoidance latencies, without altering escape, in a way similar to the reference drug diazepam (avoidance 1, mean +/- SEM, acute study: 131.1 +/- 45.5 (control), 9.0 +/- 3.3 (diazepam), 12.7 +/- 2.9 (200 mg/kg), 28.8 +/- 15.3 (400 mg/kg); chronic study: 131.7 +/- 46.9 (control), 35.8 +/- 29.7 (diazepam), 24.4 +/- 10.4 (50 mg/kg), 29.7 +/- 11.5 (200 mg/kg)). Neither EV nor EM altered measurements performed in the forced swim test, in contrast to the reference drug imipramine that significantly decreased immobility time after chronic treatment. These results were not due to motor alterations since no significant effects were detected in an open field. These observations suggest that EV exerts anxiolytic-like effects on a specific subset of defensive behaviors which have been associated with generalized anxiety disorder.

Acute Disease↗
PubMed1988

Precipitation of galactose-specific lectins by complex-type oligosaccharides and glycopeptides: studies with lectins from Ricinus communis (agglutinin I), Erythrina indica, Erythrina arborescens, Abrus precatorius (agglutinin), and Glycine max (soybean).

We have recently demonstrated that certain oligomannose and bisected hybrid type glycopeptides and bisected complex type oligosaccharides are bivalent for binding to concanavalin A and can precipitate the lectin [Bhattacharyya, L., Ceccarini, C., Lorenzoni, P., & Brewer, C.F. (1987) J. Biol. Chem. 262, 1288-1293; Bhattacharyya, L., Haraldsson, M., & Brewer, C.F. (1987) J. Biol. Chem. 262, 1294-1299]. The present results show that tri- and tetraantennary complex type oligosaccharides containing nonreducing terminal galactose residues, and a related triantennary glycopeptide, precipitate the D-galactose-specific lectins from Ricinus communis (agglutinin I) (RCA-I), Erythrina indica (EIL), Erythrina arborescens (EAL), and Glycine max (soybean) (SBA). Nonbisected and bisected biantennary complex type oligosaccharides can precipitate SBA, which is a tetrameric lectin, but not RCA-I, EIL, or EAL, which are dimeric lectins. The relative affinities of the oligosaccharides and glycopeptide were determined by hemagglutination inhibition measurements and their valencies by quantitative precipitin analyses. The equivalence points of the precipitin curves indicate that the tri- and tetraantennary oligosaccharides are tri- and tetravalent, respectively, for EIL, EAL, and SBA binding. However, the oligosaccharides are all trivalent for RCA-I binding due apparently to the larger size of the monomeric subunit of the lectin. The triantennary glycopeptide was also trivalent for RCA-I and EIL binding. Biantennary oligosaccharides with adequate chain lengths were found to be bivalent for binding to SBA; those with shorter chains did not precipitate the lectin.(ABSTRACT TRUNCATED AT 250 WORDS)

Carbohydrate Conformation↗
PubMed1982

Purification and properties of the proteinase inhibitors from Erythrina caffra (coast Erythrina) seed.

1. Four proteinase inhibitors (DE-1 to DE-4) were purified from Erythrina caffra seed by gel filtration on Sephadex G-50 followed by ion-exchange chromatography involving DEAE-cellulose and DEAE-sepharose. 2. They comprise 164-166 amino acid residues (mol. wt 18,100) including 4 half-cystine residues and resemble the Kunitz-type proteinase inhibitors. 3. The N-terminal primary structure of DE-3 revealed also homology with those of the Kunitz-type inhibitors. For DE-1, DE-2 and DE-4 no free N-terminal amino acid was found. 4. DE-1 contains a potent inhibitor for both porcine trypsin and bovine alpha-chymotrypsin. Whereas DE-2 inhibits alpha-chymotrypsin strongly and has practically no action on trypsin, DE-3 inhibits both trypsin and alpha-chymotrypsin strongly. DE-4 is a potent inhibitor for trypsin but it binds alpha-chymotrypsin only weakly.

Amino Acid Sequence↗
PubMed1981

Purification and some properties of two proteinase inhibitors (DE-1 and DE-3) from Erythrina latissima (broad-leaved erythrina) seed.

Two proteinase inhibitors, DE-1 and DE-3, were purified from Erythrina latissima seeds. Whereas DE-1 inhibits bovine chymotrypsin and not bovine trypsin, DE-3 inhibits trypsin but not chymotrypsin. The molecular weights and the amino acid compositions of the two inhibitors resemble the corresponding properties of the Kunitz-type proteinase inhibitors. The N-terminal primary structure of DE-3 showed homology with soybean trypsin inhibitor (Kunitz) and also with the proteinase inhibitors (A-II and B-II) from Albizzia julibrissin seed.

Amino Acid Sequence↗
PubMedDate not supplied

Investigation of Erythrina spp. VII. Chemical constituents of Erythrina variegata var. orientalis bark.

The petroleum ether extractive of the bark of Erythrina variegata var. orientalis was fractionated and shown to be composed of wax alcohols and wax acids, alkyl ferulates, alkyl phenolates, stigmasterol, sitosterol, campesterol and possibly citrostadienol/24-methylenelophenol. The ethanol extractive yielded chloroform-soluble and water-soluble bases, identified as erysovine and stachydrine, respectively.

Cinnamates↗
PubMed1994

Site-directed mutagenesis of the synthetic Erythrina trypsin/tissue plasminogen activator (tPA) inhibitor encoding-gene to compare the interaction of Erythrina and soybean trypsin inhibitor with tPA.

Erythrina trypsin inhibitor (ETI) has good structural and sequence homology with soybean trypsin inhibitor (STI). However, STI does not inhibit tPA. From the three-dimensional structure of ETI it was known that the N-terminus of the molecule forms a finger-like structure stabilized by hydrogen bonds and hydrophobic interactions. In addition, the N-terminal finger region is located in close proximity to the reactive site loop and the N-terminal residue (Val) is bound up in the finger region. In STI the N-terminal region is located in close proximity to the reactive site loop and is folded into a structure similar to that in ETI. It was hypothesized that the N-terminal region is stabilized as in ETI and that the N-terminal residue of STI (Asp), because of its hydrophilic nature, is not involved in the structured N-terminal finger region of this protein. This leaves Asp1 of STI free to form an ion pair with Lys60 of trypsin, when STI and trypsin interact. When amino acid sequences of trypsin and the C-terminus of tPA are aligned for optimum homology, it is seen that there are a number of insertion sequences in tPA that are thought to be accommodated in the form of protrusions. One of these can be seen to occur in the region that lies opposite the Lys60 region of trypsin. It is suggested in this work that the N-terminal Asp of STI and this protrusion of tPA sterically prevent the two proteins from approaching close enough for binding and inhibition to occur. A modified form of ETI was produced with an Asp residue N-terminal to Val to simulate the N-terminal region of STI. The active sites were titrated against trypsin and assayed against tPA. The results showed that the modified form of ETI had activity towards tPA similar to that of STI. This evidence indicates strongly that the N-terminal Asp of STI prevents its binding to and inhibiting tPA.

Amino Acid Sequence↗