Appeal No. 2001-2497 Page 9
Application No. 08/855,744
See the abstract. The proteins are disclosed to bind the target antigen via a
“biosynthetic antibody binding site” and are disclosed to optionally “include other
polypeptide sequences which function, e.g., as an enzyme, toxin, binding site, or
site for attachment to an immobilization medi[um] or radioactive atom.” Id. Thus,
Huston’s multifunctional proteins comprise separate domains that (1) bind to the
target antigen and (2) carry out enzymatic or toxic reactions.
Colcher discloses “in vivo targeting of tumors with a single-chain antigen-
binding protein.” Abstract. The disclosed protein was “composed of a variable
light-chain (VL), amino acid sequence of an immunoglobulin tethered to a
variable heavy-chain (VH) sequence by a designed peptide.” Id. This protein
was disclosed to bind to the appropriate tumor antigen. See id. Colcher
suggests that “it may be possible, for more efficient therapeutic and/or diagnostic
applications, . . . to add drugs or specific combining sites for drugs and
radionuclides (i.e., bifunctional chelates).” Page 1196.
The examiner concluded that
It would have been prima facie obvious to one of ordinary skill in
the art at the time the invention was made to apply the method of
pretargeted radiolabel of Goodwin using the functionally equivalent
bifunctional antibodies . . . which can be made as single chain as
taught by Huston et al[.] or Colcher et al[.] since Goodwin teaches
the use of bifunctional antibodies . . . and since Huston et al[.] and
Colcher et al[.] teach the advantages of having single chain
chimeric antibodies over the antibody fragment conjugates . . . with
the expected benefit of reduced immunogenicity and increased
bioavailability. See Page 3, the last paragraph of Huston et al[.]
and page 1196 of Colcher et al.
Paper No. 10, page 8.
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