104 



The conjugates contained an average of 3.6moles of ADGG per 

 mole of Con A as determined from spectral absorption at 

 395nm and Lowry protein determination. The absorption 

 spectrum was similar to those presented for ADGG-BSA con- 

 jugates and contained absorption peaks at 280nm and 395nm 

 characteristic of covalent association of the protein and 

 ADGG components. 

 Characterization 



The H-DM-ADGG-Con A conjugates were analyzed for 

 stability to hydroxlyamine under neutral conditions. By 

 this criterion they were found to contain a minimum of 78% 

 stable covalent bonds comprising the H-DM-ADGG lectin 



linkage . 



3 

 The hemagglutmating ability of the H-DM-ADGG-Con A 



and ADGG-Con A conjugates was determined with human type A 

 red blood cells. ADGG-Con A conjugates would cause agglu- 

 tination at a minimal concentration of 9.5yg/ml. The effect 

 of conjugation of H-DM-ADGG to Con A and a number of other 

 lectins with varying ligand specificities was compared 

 after the synthesis at pH 5 in phosphate buffer. Table 6 



presents the results of the agglutinations and the molar 



3 

 ratios of H-DM-ADGG to lectin that resulted from conjuga- 

 tion. In all cases significant binding of H-DM-ADGG to 

 lectin occurred. Comparison of the hemagglutination titers 

 of the H-DM-ADGG-lectin conjugates with the control value 

 for each lectin shown in parenthesis, demonstrates that the 

 hemagglutination titers of Con A, castor bean type I (CB-I) , 



