Appeal No. 1999-1355 Page 8
Application No. 08/469,786
evidence or argument shift to the applicant.” In re Rijckaert, 9 F.3d 1531, 1532, 28
USPQ2d 1955, 1956 (Fed. Cir. 1993). “Measuring a claimed invention against the
standard established by section 103 requires the oft-difficult but critical step of casting
the mind back to the time of the invention, to consider the thinking of one of ordinary
skill in the art, guided only by the prior art references and the then-accepted wisdom in
the field.” In re Dembiczac, 175 F.3d 994, 999, 50 USPQ2d 1614, 1617 (Fed. Cir.
1999).
On this record, we find that the examiner’s initial burden of presenting a prima
facie case of obviousness has not been met. Hopp describes “[a] hybrid molecule
composed of a selected . . . protein and an identification or marker peptide,” wherein
“[t]he identification peptide ideally includes two primary components: a highly antigenic
N-terminal portion; and, a linking portion to connect the identification peptide to the
protein . . . [which] is characterized by being cleavable at a specific amino acid residue
adjacent the protein molecule by use of a sequence specific proteolytic agent.” Column
2, lines 53-63. The “selected protein” portion of Hopp’s hybrid “may be . . . substantially
any . . . protein that can be expressed by a vector in a transformed host cell,” including
an enzyme, a storage protein, a transport protein, an antibody, a hormone, a toxin, etc.
Column 6, line 55 to column 7, line 25.
Whether or not Hopp’s hybrid molecule can be considered to be a hybrid
between a biologically functional non-immunoglobulin protein and an immunoglobulin is
an open question, and one we need not answer here. It is enough to note that the
examiner has failed to come to grips with fact that all of the claims on appeal require
that the non-immunoglobulin protein moiety of the hybrid protein be connected to the
carboxy terminus of the immunoglobulin moiety.
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