Appeal No. 2001-0889 Page 9
Application No. 08/459,086
Appellant argues that
the claimed antibodies . . . are raised to peptides which contain, in
addition to some overlap with the amino acid sequence used by
Chow et al., at least amino acids 46 and 47 (if not more) at the C-
terminal end. . . . [T]he presence of other amino acids at the C-
terminal end of the peptides used for antibody generation could
produce altered three-dimensional conformations within the
peptides, leading to the presentation of different epitopes, and thus
antibodies with different binding specificities.
Appeal Brief, page 10 (emphasis in original).
This argument in not persuasive. Granted, the presence of additional
amino acids could lead to the presence of other epitopes and produce antibodies
with different binding specificities. But where, as here, the peptides in question
share a high degree of identical sequence, those skilled in the art would
reasonably expect that antibodies that bound one of them would bind the other
as well. Appellant has presented no evidence to the contrary, and “[a]ttorney’s
argument in a brief cannot take the place of evidence.” In re Pearson, 494 F.2d
1399, 1405, 181 USPQ 641, 646 (CCPA 1974).
Appellant also argues that “the antibodies of the claimed invention and
those described in Chow et al. can be clearly distinguished by their neutralizing
capabilities.” Appeal Brief, page 10 (emphasis in original). That is, the
antibodies disclosed by Chow bind to IFN-β but do not neutralize its activity,
whereas “the antibodies of the claimed invention, as described throughout the
specification, possess neutralizing activity toward IFN-β.” Id., page 11 (emphasis
in original). Appellant concedes that claim 7 does not expressly limit the claimed
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