Appeal No. 2006-2556 Page 5
Application No. 09/977,155
page 3. Appellants urge that the 85 kDa carboxyl-terminal fragment visualized by
Western blotting “is released from the membrane not by the protease, but rather by
subsequent biochemical extraction.” Id. at page 4
Appellants point out that “[i]n Willnow, protease cleavage at the N-terminal,
extracellular region IV processing site yields a membrane-bound fragment. The
membrane-bound C-terminal cleavage produc[t] is then biochemically extracted from
the membrane. In contrast, our claims require that cleavage by the protease release
the tail from the membrane, which does not and cannot occur in Willnow's work.” Id.
(emphasis in original).
"To anticipate a claim, a prior art reference must disclose every limitation of the
claimed invention, either explicitly or inherently." In re Schreiber, 128 F.3d 1473, 1477,
44 USPQ2d 1429, 1431 (Fed. Cir. 1997).
In our view, the examiner has not shown that Willnow discloses a protease that
cleaves the transmembrane domain of an LDL receptor, resulting in release of the
C-terminal tail from the cell membrane. We therefore agree with Appellants that the
examiner has not demonstrated that Willnow anticipates claim 1.
We agree with Appellants that claim 1 requires the protease to “release[] the tail
from the membrane.” The only tail recited in claim 1 is the C-terminal tail. Thus, claim 1
explicitly requires the cleavage of the protein to release the C-terminal tail from the cell
membrane.
The protease disclosed in Willnow cleaves the extracellular portion of the LRP.
Willnow, Figure 1 (cleavage site in region IV indicated by arrows). By cleaving the
extracellular portion of the protein, Willnow’s protease leaves the entire C-terminal
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