Neuraminidases immobilized

Neuraminidase, immobilized on Agarose4B Origin Clostridium perfringens Fluka... 

Neuraminidase has been immobilized on a number of matrices and the kinetic and stability properties of the preparations reported. Optimal conditions for the use of neuraminidase, immobilized on agarose cyclic imido-carbonate, for the desialylisation of glycoconjugates have been established with... 

Investigation of the binding characteristics of urinary acid 3-D-gaIactosidase, 3-D-2-acetamido-2-deoxyglucosidase, a-D-galactosidase and a-L-fucosidase from patients with mucolipidosis II and mucolipidosis III to agarose-immobilized concanavalin A revealed a two to ten-fold decrease in the proportion of enzyme (that adsorbed on the lectin) activities from patients with mucolipidoses II and III. Neuraminidase treatment of the unabsorbed enzyme fraction did not... 

The inner surface of nylon tubing has been activated with dimethylsulphate and then treated with L-lysine. After activation of the derivatized surface with glutaraldehyde or dimethyl adipimidate, neuraminidase was covalently linked to the surface of the tubing. The stability of the active immobilized enzyme was investigated and its potential application for release of neuraminic acid from surfaces of leukaemic AKR mouse thymus and spleen lymphocytes evaluated. 

From the clinical point of view, the potential ability of liposome-encapsulated enzymes to enter the cytoplasm or lyso-somes of live cells is of primary importance for the treatment of inherited diseases caused by the abnormal functioning of some intracellular enzymes, especially in liver and CNS cells. The use of liposome-immobilized enzymes instead of their native precursors opens new opportunities for enz)une therapy especially in the treatment of diseases localized in liver cells that are natural targets for liposomes. Thus, the biodistribution of liposomes made of phosphatidylcholine, phospha-tidic acid, and cholesterol (in 7 1 2 molar ratio) and containing jS-fructofuranosidase has been studied. It was shown that within an hour, 50% of the administered enzyme can still be found in the circulation, and the enzyme preserves its activity for a long time — 25% of the administered activity can be found in the liver after 48 hours. Similar data have been obtained for intravenously administered liposome-encapsulated a-mannosidase and neuraminidase. ... 

The extents of sialylation of eleven plasma hydrolases have been examined. Most plasma hydrolases e.g. a-L-fucosidase and a-D-mannosidase) were eluted from DEAE-cellulose at a lower salt concentration after treatment with neuraminidase, although the elution profiles of p-D-glucosidase, P-D-xylosidase, and acid phosphatases were unaffected, indicating that they are less susceptible to the action of neuraminidase. The structure (9) assigned (G. Spick, B. Bayard, B. Fournet, and G. Strecker, F.E.B.S. Letters, 1975, 50, 296) to the carbohydrate component of human serotransferrin has been confirmed by high-resolution H n.m.r. spectroscopy. Electrophoresis separated human serotransferrin into four molecular forms that contain different proportions of bound iron. The nature of the interaction of renins from human and rabbit kidneys with immobilized concanavalin A, and their subsequent desorption with methyl a-D-mannopyrano-side, suggested that both proteins are glycosylated. ... 

Structural Elucidation via Sequential Enzymatic Degradation A sequential exogly-cosidase treatment of immunoglobulins allows a more detailed identification of oligosaccharide structures [620]. For this purpose, immobilized proteins are treated with carbohydrate-specific enzymes such as neuraminidase, which... 

Neuraminidase has been immobilized to give a water-insoluble derivative with retention of enzymic activity by covalent reaction with agarose cyclic imidocarbonate, a hydrazide derivative of agarose cyclic imidocarbo-nate, and periodate-oxidized controlled-pore glass (CPG)-glycophase. ... 

A rapid procedure involving affinity chromatography on immobilized fetuin has been used to remove contaminating proteases from commercial preparations of neuraminidase. " The affinity-adsorbed enzyme was virtually free from protease activity, and the use of protease-free neuraminidase in studies of the metabolism of desialylized glycoproteins and of tumour cells was discussed. 

An affinant for neuraminidase, which was formed by reaction of ai-acid glycoprotein with agarose cyclic imidocarbonate, did not display non-specific adsorption that is characteristic of the analogous oxamic acid derivatives. Concanavalin A immobilized on agarose cyclic imidocarbonate effected different bindings, depending on whether or not ethylene glycol was present. ... 

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