Appeal No. 2002-2030 Page 7
Application No. 09/294,663
fifteen expressed proteins that were bound by antibody to T. ni IIM. See pages
31-33. Of the fifteen cross-reacting proteins, however, only eight had a
molecular weight similar to that of T. ni IIM. See page 33. Since the structure,
and therefore the size, of a protein is a function of the DNA that encodes it, the
differing sizes of the cross-reacting proteins indicate that the two cDNAs isolated
from T. ni are not representative of IIM-encoding DNAs as a genus.
Thus, the evidence supports the examiner’s position that a description of
two T. ni IIM cDNAs is inadequate to describe the full genus of IIM-encoding
genes encompassed by claim 1. Rather, claim 1’s recitation of “a gene encoding
an invertebrate intestinal mucin (IIM) protein” falls squarely within the category of
nucleic acids defined by function, not structure, that were disparaged by the Lilly
court. See 119 F.3d at 1568, 43 USPQ2d at 1406 (“A definition by function, as
we have previously indicated, does not suffice to define the genus because it is
only an indication of what the gene does, rather than what it is.”). We therefore
agree with the examiner that claims 1, 6, and 9 are not adequately described by
the instant specification.
Appellants argue that the specification “substantially defines the essential
physical and structural features that characterize IIM proteins.” Appeal Brief,
page 17. Appellants point to the specification’s disclosure that the proteins
encoded by the isolated T. ni cDNAs
have an amino acid composition similar to that of a typical
vertebrate mucin, . . . and exhibiting the characteristics of high
glycosylation, high resistance to protease, stability over a wide pH
range, and the presence of strong intermolecular sulfide bonds.
The IIM proteins in particular further are characterized by localized
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