bauhinia carronii/carbohydrate

Lyen an sove nan clipboard la

AtikEsè klinikPatant

Chwazi kalite sòt

Paj 1 soti nan 62 rezilta yo

Parallel synthesis and screening of a solid phase carbohydrate library.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

A solid phase carbohydrate library was synthesized and screened against Bauhinia purpurea lectin. The library, which contains approximately 1300 di- and trisaccharides, was synthesized with chemical encoding on TentaGel resin so that each bead contained a single carbohydrate. Two ligands that bind

Self-assembled carbohydrate-based vesicles for lectin targeting.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

This study examined the physicochemical interactions between vesicles formed by phosphatidylcholine (PC) and glycosylated polymeric amphiphile N-acetyl-β-d-glucosaminyl-PEG900-docosanate (C22PEG900GlcNAc) conjugated with Bauhinia variegata lectin (BVL). Lectins are proteins or glycoproteins capable

A chimeric lectin formed from Bauhinia purpurea lectin and Lens culinaris lectin recognizes a unique carbohydrate structure.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

Lectins are carbohydrate-binding proteins widely used in biochemical, immunochemical, and histochemical studies. Bauhinia purpurea lectin (BPA) is a leguminous lectin with an affinity for galactose and lactose. Nine amino acids, DTWPNTEWS, corresponding to the amino acid sequence from aspartic

Determination of the carbohydrate-binding site of Bauhinia purpurea lectin by affinity chromatography.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

To determine the carbohydrate-binding site of Bauhinia purpurea lectin (BPA), a D-galactose- and lactose-binding lectin, a peptide which interacts with lactose was purified from endoproteinase Asp-N digests of BPA by chromatography on a lactose-Sepharose column. It consists of nine amino acids and

Carbohydrate-binding specificities of five lectins that bind to O-Glycosyl-linked carbohydrate chains. Quantitative analysis by frontal-affinity chromatography.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

The carbohydrate-binding specificities of lectins purified from Agaricus bisporus (ABA-I), Arachis hypogaea (PNA), Bauhinia purpurea (BPA), Glycine max (SBA), and Vicia villosa (VVA-B4) have been studied by affinity chromatography on columns of the immobilized lectins, and quantitatively analyzed by

Pneumocystis carinii: surface reactive carbohydrates detected by lectin probes.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

Pneumocystis carinii obtained from rat lungs (RLH) and in vitro culture (RTC) were reacted with a panel of 14 fluorescein isothiocyanate conjugated lectins. Percentage fluorescence and fluorescent intensity were determined for both trophic and cyst forms. All RLH and RTC derived organisms bound

Detection of surface carbohydrates on Pneumocystis carinii by fluorescein-conjugated lectins.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

Lectins react with a wide range of different carbohydrates (Table 1). Even so-called monospecific anti-H(O) lectins from Lotus tetragonolobus, Ulex europaeus, and Anguilla anguilla react not only with the anti-H determinant but also with several fucosylated carbohydrates. Consequently, the type of

Flow cytometric analyses of lectin binding to Pneumocystis carinii surface carbohydrates.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

Pneumocystis carinii obtained from infected rat lung homogenates was incubated with fluorescein isothiocyanate-conjugated lectins, counterstained with the nuclear stain, propidium iodide (PI), and analyzed by dual parameter histograms for lectin-associated green and PI-associated red fluorescence

Carbohydrate and peptide antigens in macrophage populations derived from human bone marrow and milk: an immunomorphological and immunochemical analysis.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

An immunomorphological and immunochemical study was performed to elucidate the pattern of carbohydrate antigens and their relationships to the cluster differentiation (CD) 68 epitopes on macrophages derived from human bone marrow and milk. Core and backbone antigens recognized by lectins from

Flow cytometric analysis of lectin binding to in vitro-cultured Perkinsus marinus surface carbohydrates.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

Parasite surface glycoconjugates are frequently involved in cellular recognition and colonization of the host. This study reports on the identification of Perkinsus marinus surface carbohydrates by flow cytometric analyses of fluorescein isothiocyanate-conjugated lectin binding. Lectin-binding

Nonstatistical binding of a protein to clustered carbohydrates.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

Carbohydrate-derivatized self-assembled monolayers (SAMs) are used as a model system to address issues involving cell-surface carbohydrate-protein interactions. Here we examine the influence of carbohydrate surface density on protein-binding avidity. We show that the binding selectivity of Bauhinia

Purification and characterization of a carbohydrate-binding peptide from Bauhinia purpurea lectin.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

In order to examine the correlation between the amino acid sequence and sugar binding specificity of Bauhinia purpurea lectin (BPA), a galactose and lactose binding lectin, a peptide which interacts with lactose was purified from an Asp-N endoproteinase digest of BPA by means of affinity

Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

A chimeric lectin gene was constructed by using a cDNA clone coding the Bauhinia purpurea lectin (BPA) in which a part of the metal-binding region was replaced by the corresponding region of the mannose-binding Lens culinaris lectin (LCA). The chimeric lectin expressed in Escherichia coli was found

Further characterization of some heterophile agglutinins reacting with alkali-labile carbohydrate chains of human erythrocyte glycoproteins.

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

The nature of the receptor sites for several agglutinins is characterized by hemagglutination inhibition assays. The inhibitory activity of human erythrocytes glycoproteins, from which sialic acid, sialic acid and galactose or alkali-labile oligosaccharides have been removed, is compared to the

Recognition profile of Bauhinia purpurea agglutinin (BPA).

Se sèlman itilizatè ki anrejistre yo ki ka tradwi atik yo

Bauhinia purpurea agglutinin (BPA) is a Galbeta1-3GalNAc (T) specific leguminous lectin that has been widely used in multifarious cytochemical and immunological studies of cells and tissues under pathological or malignant conditions. Despite these diverse applications, knowledge of its carbohydrate

Antre nan paj
facebook nou an

Herbal & Natural Medicine

Baz done ki pi konplè remèd fèy medsin te apiye nan syans

Travay nan 55 lang
Geri èrbal te apiye nan syans
Remèd fèy rekonesans pa imaj
Kat entèaktif GPS - tag zèb sou kote (vini byento)
Li piblikasyon syantifik ki gen rapò ak rechèch ou an
Search remèd fèy medsin pa efè yo
Izeganize enterè ou yo ak rete kanpe fè dat ak rechèch la nouvèl, esè klinik ak rive

Tape yon sentòm oswa yon maladi epi li sou remèd fèy ki ta ka ede, tape yon zèb ak wè maladi ak sentòm li itilize kont.
* Tout enfòmasyon baze sou rechèch syantifik pibliye