Appeal No. 2005-1383
Application No. 09/364,847
First, we point out that claims 5 and 6 are in a product-by-process format. The
appellants are advised that an invention defined in this manner is a product and not a
process. In re Thorpe, 777 F.2d 695, 697, 227 USPQ 964, 966 (Fed. Cir. 1985). Thus,
it is the patentability of the product which must be considered. In the case before us,
we do not find, and the appellants have not pointed out, any characteristics which
distinguish the protein fusion recited in claims 5 and 6 from that which is recited in claim
1. That is, the fusion protein of claim 1 does not automatically change when it is
expressed in a plant cell or in bacteria. Thus, the reasons for our finding the fusion
protein of claim 1 unpatentable over the teachings of Peoples and Bülow apply with
equal force to claims 5 and 6 because they are directed to the same composition.
Second, even if we assume arguendo, that claims 5 and 6 are directed to a
method of expressing the fusion protein in a plant cell or a bacterium, we would find the
appellants’ argument unconvincing. We point out that Bülow discloses the expression
of the recombinant bifunctional enzymes in bacteria (E. coli). More importantly, both the
specification (p. 1, lines 13-14) and Peoples discloses that PHA is naturally produced in
bacteria (e.g., col. 2, lines 50-52). Peoples further discloses the isolation and
expression of numerous genes which encode catalytically active enzymes involved in
the PHA biosynthetic pathway in bacteria (e.g., col. 3, lines 38-41, lines 50-64; col. 12,
lines 19-51; col. 14, lines 20-33; col. 16, lines 16-56; col. 19, lines 23-60; Tables 2 and
3). Peoples still further discloses that the genes encoding the thiolase, reductase
and/or polymerase for PHA can be expressed in plants to produce the desired product
(e.g., col. 3, lines 38-41, lines 44-49 and lines 63-66; col. 26, lines 42-46). Thus,
assuming arguendo that claims 5 and 6 were directed to the expression of the protein
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