maackia/carbohydrate

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A unique amino acid sequence involved in the putative carbohydrate-binding domain of a legume lectin specific for sialylated carbohydrate chains: primary sequence determination of Maackia amurensis hemagglutinin (MAH).

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The primary sequence of 247 amino acids of Maackia amurensis hemagglutinin (MAH) was determined using a protein sequencer. After digestion with endoproteinase Lys-C, Asp-N, Arg-C, or Glu-C of MAH, the resulting peptides were purified by reversed phase high performance liquid chromatography (HPLC)

Studies by site-directed mutagenesis of the carbohydrate-binding properties of a bark lectin from Robinia pseudoacacia.

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A bark lectin, RBL, from Robinia pseudoacacia (black locust), binds galactose-related sugars specifically. Recombinant RBL (rRBL) with a histidine tag was expressed in Escherichia coli, purified and characterized. rRBL agglutinated rabbit erythrocytes and the hemagglutination was inhibited by

A potential endogenous ligand of annexin IV in the exocrine pancreas. Carbohydrate structure of GP-2, a glycosylphosphatidylinositol-anchored glycoprotein of zymogen granule membranes.

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We demonstrated previously that annexins IV, V, and VI, proteins of the calcium/phospholipid-binding annexin family, have glycosaminoglycan binding properties (Ishitsuka, R., Kojima, K., Utsumi, H., Ogawa, H., and Matsumoto, I. (1998) J. Biol. Chem. 273, 9935-9941). In this study, we investigated

Selenium Protects Retinal Cells from Cisplatin-Induced Alterations in Carbohydrate Residues.

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BACKGROUND Investigate alterations in the expression and localization of carbohydrate units in rat retinal cells exposed to cisplatin toxicity. OBJECTIVE The aim of the study was to evaluate putative protective effects of selenium on retinal cells subjected to cisplatin. METHODS Animal

Carbohydrate antigens of pig tissues reacting with human natural antibodies as potential targets for hyperacute vascular rejection in pig-to-man organ xenotransplantation.

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Pig tissues were screened by immunofluorescence with lectins, mAb, and human natural antibodies for the presence of carbohydrate antigens, which may be potential targets for hyperacute vascular rejection in pig to man xenotransplantation. The unfucosylated monomorph linear B-antigen was found at the

Differences in cell surface carbohydrates, and in laminin and fibronectin synthesis, between adherent and non-adherent Ehrlich ascites tumor cells.

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Differences in cell surface carbohydrates and in laminin and fibronectin synthesis between 2 Ehrlich ascites tumor (EAT) cell lines, the adherent and non-adherent EAT cells, have been studied. The adherent EAT (a-EAT) cells grow in monolayer in vitro in the presence of fetal bovine serum. The

Lotus tetragonolobus, Ulex europaeus, Maackia amurensis, and Arachis hypogaea (peanut) lectins influence the binding of Helicobacter pylori to gastric carbohydrates.

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BACKGROUND The carbohydrates of gastric mucins and other sugar structures are involved in interactions with Helicobacter pylori (H. pylori) adhesins. The binding of bacteria to mucins can protect the epithelium from direct contact with the pathogen and from developing infection because of a specific

Detection of carbohydrate-binding proteins by oligosaccharide-modified polypyrrole interfaces using electrochemical surface plasmon resonance.

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This paper reports on the use of electrochemical surface plasmon resonance (E-SPR) for the detection of carbohydrate-binding proteins. The generation of an SPR sensor specific to lectins Arachis hypogaea (PNA) and Maackia amurensis (MAA) is based on the electrochemical polymerization of

Carbohydrate moieties of N-cadherin from human melanoma cell lines.

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Expression of N-cadherin an adhesion molecule of the cadherin family, in tumor cells is associated with their increased invasive potential. Many studies suggested the role of N-linked oligosaccharides as important factors that contribute to metastasis by influencing tumor cell invasion and adhesion.

Differences in terminal carbohydrate structures of sialomucin in the murine nasal cavity.

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Terminal carbohydrate structures of sialomucin in the murine nasal cavity were characterized by means of lectin histochemistry. Two kinds of biotinylated lectins (Maackia amurensis agglutinin and Sambucus nigra agglutinin), which recognize sialic acid residues, showed marked differences in their

Characterization of carbohydrate chains of C1-inhibitor and of desialylated C1-inhibitor.

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Carbohydrate chains of C1-inhibitor were identified with a binding assay using different lectins. Lectins from Sambucus nigra (SNA) and Maackia amurensis (MAA) that are specific for sialic acids bound to C1-inhibitor. Lectin from Datura stramonium (DSA) reacted also with the inhibitor indicating

[Carbohydrate structure of glycoconjugate in the murine eustachian tube pharyngeal orifice].

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In this study, neuraminidase (sialidase) and 6 different lectins, wheat germ agglutinin (WGA), Limax flavus agglutinin (LFA), Sambucus nigra agglutinin (SNA), Maackia amurensis agglutinin (MAA), peanut agglutinin (PNA), and Amaranthin, were used to histochemically characterize the carbohydrate

Haptoglobin glycoforms in a case of carbohydrate-deficient glycoprotein syndrome.

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Alterations in haptoglobin (Hp) glycosylation were examined in the plasma of the first patient with carbohydrate-deficient glycoprotein syndrome (CDGS) who was described in Poland. Hp concentration in the CDGS patient plasma was low (240 mg/l) and the Hp phenotype was shown to be 2-2. Three

Characterization of the carbohydrate binding specificity and kinetic parameters of lectins by using surface plasmon resonance.

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An accurate, rapid, and sensitive method for characterizing the carbohydrate binding properties of lectins using a BIAcore apparatus and the detection method of surface plasmon resonance is described. As a model study, the sialic acid binding lectins from Sambucus nigra and Maackia amurensis, which

Differences in carbohydrate composition of FSH preparations detected with lectin-ELISA systems.

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FSH is a glycoprotein containing N-linked carbohydrates which exhibit a variety of forms ranging from mono- to multibranched structures. Variation in glycosylation, particularly the degree of terminal sialylation, determines the half-life of the hormone and hence its in vivo bioactivity. The

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