Ex parte ROBINSON - Page 5




              Appeal No. 1995-2903                                                                                         
              Application No. 07/693,055                                                                                   


                     the method of detecting anti-viral glycoprotein antibodies as disclosed by                            
                     NEURATH . . . .                                                                                       
                     We have carefully considered the evidence and discussion in support of the                            
              rejection presented by the examiner.  The examiner has determined that the ability of lectin                 
              to bind viral glycoprotein, as described by Larson, is sufficient to equate it to the                        
              antibodies similarly used by Neurath.  In our opinion, commonality of this single                            
              characteristic is insufficient to establish that lectin and the binding antibodies of Neurath                
              are equivalent or interchangeable in an immunoassay method as claimed.   The examiner                        
              has provided no evidence to demonstrate that lectin and the antibodies of Neurath would                      
              have been recognized, by those of ordinary skill in this art, as equivalent for any purpose                  
              and particularly as a binding material on an assay surface for use in an immunoassay.                        
                     As motivation the examiner states that the substitution of lectin for the binding                     
              antibody of Neurath (Answer, page 10):                                                                       
                     . . . would afford the artisan a readily available means whereby a generic                            
                     binding agent that is immobilized or coated on to a solid support or assay                            
                     surface is used to immobilizing viral glycoproteins thereon.  Additionally, it is                     
                     noted that by using a lectin coated support instead of an antibody-coated                             
                     support, one need not develop a new specific binding member when one                                  
                     wishes to immobilize the viral glycoproteins from a variety of viruses.                               
                     Accordingly, this reduction in the variety of starting materials would readily                        
                     translate into a less expensive assay, thereby providing commercial                                   
                     incentives for the combination of the prior art of record.                                            
              We have no doubt that Neurath could be modified in the manner described by the                               
              examiner and would result in the advantages described.  However, we find no suggestion                       
              to do so other than appellant's specification. (Note the Specification page 4, lines 6-14                    

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