Figure 5

Characteristics of PLAP-scFv binding in the presence of competing isozymes. 5A.A fixed amount of biotinylated-PLAP was incubated with immobilized soluble scFv of the clone GLE4. The extent to which this could be inhibited by varying concentrations of competing isozymes was measured. Binding in the absence of any competing isozyme was taken as 100%. The binding to biotinylated-PLAP is inhibited only by unbiotinylated PLAP and not the other two isozymes of alkaline phosphatase. The labels on x-axis represent the molar concentration of the various isozymes included in the experiment. 5B.Competition of PLAP-GLD6 binding by IAP and BAP. Normalisation of the data was done as in Figure 6A. The binding to biotinylated-PLAP is inhibited by the two isozymes (BAP and PLAP) but not the third. The labels on x-axis represent the molar concentration of the various isozymes included in the experiment. 5C.Competition of PLAP-GL2D binding by IAP and BAP. Normalisation of the data was done as in Figure 6A. Binding to biotinylated-PLAP binding was inhibited by all the isozymes of alkaline phosphatase. At the maximum concentration of competing isozyme studied, the inhibition was the same. However, there was a slight difference in the relative affinity when 50 % inhibition was calculated. The labels on x-axis represent the molar concentration of the various isozymes included in the experiment.