Abstract
Sialidase assays were carried out with the substrate, ganglioside G D1a, coated onto enzyme immunoassay plate wells. Following the incubation of G D1a with sialidase from V. cholerae, the amount of ganglioside G M1 produced was measured as follows: cholera toxin B subunit conjugated to horseradish peroxidase was added to specifically bind to G M1, and then the amount of bound peroxidase was determined in a colorimetric enzymatic assay. In the absence of detergent, linearity for the detection of G M1 was 0 to 0.5 pmol per well, and the sensitivity for sialidase detection was about 3 fmol of product formed per minute. The addition of detergent (Triton CF-54) to the assay reduced the sensitivity and increased the amount of substrate required. Application of this assay for the detection of cell-derived neutral (pH 6.5) sialidase activities in the conditioned medium of human skin fibroblasts is described.
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