114 

 ADGG that were available. The number of molecules bound 



over a 15 minute period at 22°C was compared to the amount 



125 

 of I-Con A bound at equivalent concentrations. The 



results are presented in Table 7. The H-7 cells bound 



identical amounts of either Con A derivative (10 x 10 



molecules/cell). The binding of both was 87-89% inhibi- 



table by 30 minutes preincubation with Con A (lOOpg/ml) 



and 76-85% inhibitable by ImM MDM. ADGG (2 x 10~ 6 M) did 



3 125 



not interfere with the binding of H-DM-ADGG-Con A or I- 



Con A further establishing that the conjugates interact 



with cell surface glycoproteins by virtue of specific 



binding of the Con A portion of the conjugate. 



Competition of ADGG-Con A or Con A with the binding 



125 

 of I-Con A by H-7 CHO cells is presented m Figure 25. 



125 

 A constant amount of I-Con A was competed with increasing 



amounts of ADGG-Con A or Con A. The data is presented as 



125 

 the fraction I-Con A bound versus the fraction of compe- 

 titor Con A of the total Con A present. The linearity of 

 the data and the near identical results obtained for both 

 competitors clearly identify the sites for cellular binding 

 of ADGG-Con A as being identical with those for Con A. 



The actual uptake and internalization of ADGG-Con A by 

 H-7 CHO cells was quantitated by exposing cells under sterile 

 conditions to H-DM-ADGG-Con A as previously described for 

 cell binding assays. After washing the cells as if for 

 determination of bound material, fresh culture media was 

 added instead and the cells returned to 37°C for 60 minutes. 



