Comparison of beta-D-galactosidase from Escherichia coli and horseradish peroxidase as labels of anti-human ferritin Fab' by sandwich enzyme immunoassay technique.
beta-D-Galactosidase from Escherichia coli and horseradish peroxidase were compared as labels of anti-human ferritin Fab' by sandwich enzyme immunoassay technique using fluorogenic substrates for enzyme assay. The anti-human ferritin Fab'-peroxidase conjugates gave lower nonspecific bindings and higher specific bindings than the corresponding Fab'-beta-D-galactosidase conjugates. As a result, the former provided more sensitive dose response curves for human ferritin than the latter. However, the peroxidase conjugates were required in a larger quantity, since peroxidase assay was much less sensitive than beta-D-galactosidase assay.
D000906:Antibodies; D004926:Escherichia coli / Q000201:enzymology; D005293:Ferritins / Q000276:immunology*; D005696:Galactosidases; D006735:Horseradish Peroxidase / Q000378:metabolism; D006801:Humans; D007124:Immunoenzyme Techniques; D007140:Immunoglobulin Fab Fragments; D007700:Kinetics; D010544:Peroxidases; D001616:beta-Galactosidase / Q000378:metabolism
D000906:Antibodies; D007140:Immunoglobulin Fab Fragments; D005293:Ferritins; D006735:Horseradish Peroxidase; D010544:Peroxidases; D005696:Galactosidases; D001616:beta-Galactosidase