canavalia/phosphatase

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An interaction between human seminal acid phosphatase and Canavalia gladiata DC lectin.

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Interactions between human seminal acid phosphatase (AcP) and five kinds of lectins were studied. Seminal plasma was mixed with the lectins at various ratios. The mixtures were centrifuged and the supernatants were assayed for AcP activity. The activity was effectively reduced only with Canavalia

Binding sites of seminal acid phosphatase to Canavalia gladiata DC lectin.

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Binding sites of seminal acid phosphatase (AcP) to Canavalia gladiata DC lectin (Can G) were examined. Complex of AcP and Can G produced in a test tube was solubilized with alpha-methyl-D-mannoside and was fractionated with Sephadex G-200. The elution pattern of AcP activity of the complex was

The major Kurloff cell glycoproteins: lectin affinities, glycosidase susceptibilities and relationship with the sialylated acid phosphatases of the Kurloff body.

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Urea-soluble fractions from purified Kurloff cells (KC) were analysed by affinoblotting. Lectin reactivities were quasi-exclusively confined to the 30-35 kDa major glycoproteins (mGPs) (responsible for the PAS positivity of the Kurloff body) with strong affinities for Canavalia ensiformis lectin,

O- and N-glycosylation of the Leishmania mexicana-secreted acid phosphatase. Characterization of a new class of phosphoserine-linked glycans.

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The protozoan parasite Leishmania mexicana secretes a heavily glycosylated 100-kDa acid phosphatase (sAP) which is associated with one or more polydisperse proteophosphoglycans. Most of the glycans in this complex were released using mild acid hydrolysis conditions that preferentially cleave

Studies on phosphatases from jack bean (Canavalia ensiformis).

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[Lectins as reagents for the differentiation of serum enzymes. Lectins as reagents, I. (author's transl)].

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Lectins from Canavalia ensiformis, Phaseolus vulgaris, and Triticum vulgare react with arylamidase, alkaline phosphatase, gamma-glutamyltransferase, and cholinesterase of human sera by formation of enzymatically active, mostly insoluble complexes. Arylamidase, alkaline phosphatase, and

[Catalytic concentration, multiple forms, and lectin affinity of microsomal enzymes from human tissues: lectins as reagents, II (author's transl)].

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We estimated the concentrations, multiple forms, and lectin binding of five microsomal enzymes in particle free extracts from human kidney, pancreas, jejunal mucosa, and normal and cancerous liver. While arylesterase markedly reacted only with concanavalin A, arylamidase, alkaline phosphatase,

Galectin-1-mediated cell adhesion, invasion and cell death in human anaplastic large cell lymphoma: regulatory roles of cell surface glycans.

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Galectin-1 is known to be one of the extracellular matrix proteins. To elucidate the biological roles of galectin-1 in cell adhesion and invasion of human anaplastic large cell lymphoma, we performed cell adhesion and invasion assays using the anaplastic large cell lymphoma cell line H-ALCL, which

[Lectin-binding proteins of plasma membranes of a human trophoblast].

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Spectra of lectin-binding proteins of the human trophoblast were studied by the method affinity blotting using a set of loctins conjugated with peroxidase. The set included lectins Lens culinaris (LcL), Canavalia ensiformis (Con A), Ricinus communis (RCA 1), Arachis hypogaea (PNA), Triticum vulgaris

Specific inhibition of urease by N-acylphosphoric triamides.

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Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50%

Characterization of alpha-mannosidase from Erythrina indica seeds and influence of endogenous lectin on its activity.

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alpha-mannosidase from Erythrina indica seeds is a Zn(2+) dependent glycoprotein with 8.6% carbohydrate. The enzyme has a temperature optimum of 50 degrees C and energy of activation calculated from Arrhenius plot was found to be 23 kJ mol(-1). N-terminal sequence up to five amino acid residues was

Jaburetox affects gene expression and enzyme activities in Rhodnius prolixus, a Chagas' disease vector.

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Jaburetox, a recombinant peptide of ∼11kDa derived from one of the Canavalia ensiformis (Jack Bean) urease isoforms, is toxic and lethal to insects belonging to different orders when administered orally or via injection. Previous findings indicated that Jaburetox acts on insects in a complex

A comparison of the short and long term effects of insecticidal lectins on the activities of soluble and brush border enzymes of tomato moth larvae (Lacanobia oleracea).

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When fed in semi-artificial diet in short- and long-term bioassays, the lectins from snowdrop (Galanthus nivalis; GNA) and jackbean (Canavalia ensiformis; Con A) affected the activities of soluble and brush border membrane (BBM) enzymes in the midgut of Lacanobia oleracea larvae. In the short term

Jaburetox, a urease-derived peptide: Effects on enzymatic pathways of the cockroach Nauphoeta cinerea

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Jaburetox is a recombinant peptide derived from one of the Canavalia ensiformis urease isoforms. This peptide induces several toxic effects on insects of different orders, including interference on muscle contractility in cockroaches, modulation of UDP-N-acetylglucosamine pyrophosphorylase (UAP) and

The determination of the anomeric configuration of glycosyl-phosphoryl linkages of immunogenic phosphoglycans.

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Phosphoglycans from the cell wall of many strains of Streptococci contain terminal carbohydrate units linked by phosphodiester bridges to other residues of the glycans. In the immune response to phosphoglycans, the terminal carbohydrate-phosphate moieties function as antigenic determinants and

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