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Sialidase antibodies

Roggentin, P., Gutschker-Gdaniec, G.H.M., Hobrecht, R., and Schauer, R., 1988b, Early diagnosis of clostridial gas gangrene using sialidase antibodies, Clin. Chim. Acta 173 251-262. [Pg.307]

It is at present unclear whether the different clearing-mechanisms of rabbit erythrocytes observed after treatment with sialidase and a-D-galactosidase, respectively, are mediated by two different antibodies, one causing sequestration by macrophages after deposition of C3b complexes on the erythrocyte surface as the second step in the aforementioned mechanism, and the other leading to intravascular destruction of erythrocytes by activation of the whole complement cascade. [Pg.224]

IgG receptors on cultured, human lymphocytes.526 Sialidase treatment of lymphocytes from sensitized subjects increased the responsiveness to viral, bacterial, and fungal antigens.527 The same treatment of human, Herpes simplex virus-infected cells was found to enhance the sensitivity of the cells to lysis mediated by antibody and complement.528... [Pg.229]

M. S. Leguizamon, O. E. Campetella, S. M. Gonzalez-Cappa, and A. C. C. Frasch, Mice infected with Trypanosoma cruzi produce antibodies against the enzymatic domain of trans-sialidase that inhibit its activity, Infect. Immun., 62 (1994) 3441—3446. [Pg.366]

Gruen, L., et al. (1993). Determination of Relative Binding Affinity of Influenza Virus N9 Sialidases with the Fab Fragment of Monoclonal Antibody NC41 Using Biosensor Technology, Eur. J. Biochem. 217 319—325. [Pg.46]

L. Ratier, M. Unutia, G. Paris, L. Zarebski, A. C. Fiaseh, and F. A. Goldbaum, Relevance of die diversity among members of die Trypanosoma cruzi trans-sialidase femily analyzed widi eamehds single-domain antibodies, PLoS ONE, 3 (2008) e3524. [Pg.477]

FIGURE 5. Thin section of human colon overlaid with influenza C virus. Bound virus was visualized by an immunoassay with FITC-conjugated anti-influenza antibodies. (Top) Normal staining (Bottom) same as a after sialidase treatment. [Pg.20]

Kojima, N., Handa, K., Newman, W., and Hakomori, S., 1992a, Multi-recognition capability of E-selectin in a dynamic flow system, as evidenced by differential effects of sialidases and anticarbohydrate antibodies on selectin-mediated cell adhesion at low vs. high wall shear stress A preliminary note, Biochem. Biophys. Res. Commun. 189 1686-1694. [Pg.258]


See other pages where Sialidase antibodies is mentioned: [Pg.210]    [Pg.109]    [Pg.361]    [Pg.440]    [Pg.210]    [Pg.109]    [Pg.361]    [Pg.440]    [Pg.139]    [Pg.224]    [Pg.225]    [Pg.492]    [Pg.524]    [Pg.167]    [Pg.317]    [Pg.335]    [Pg.336]    [Pg.21]    [Pg.327]    [Pg.333]    [Pg.339]    [Pg.341]    [Pg.343]    [Pg.347]    [Pg.347]    [Pg.368]    [Pg.487]    [Pg.494]    [Pg.728]    [Pg.181]    [Pg.59]    [Pg.60]    [Pg.414]    [Pg.417]    [Pg.439]    [Pg.86]    [Pg.88]    [Pg.90]    [Pg.1352]    [Pg.1939]    [Pg.1968]    [Pg.34]    [Pg.131]    [Pg.266]   
See also in sourсe #XX -- [ Pg.339 , Pg.343 ]




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