Appeal No. 2006-2556 Page 4
Application No. 09/977,155
related protein (LRP). Answer, page 3 (citing Willnow, abstract). Willnow uses the
truncated forms of the LRP to study the ligand binding properties of the receptor.
See Willnow, abstract, and paragraph spanning pages 15287-15288.
The LRP-minireceptors prepared by Willnow are composed of either region II or
region IV of the extracellular domain of the LRP, fused to the transmembrane portion of
the protein and the C-terminal cytoplasmic tail. Willnow, page 15828, right column, first
paragraph, and Figure 1. Thus, Willnow’s modifications of the LRP are all in the
portions of the protein outside the cell membrane, between the transmembrane domain
and the N-terminus. See Willnow, Figure 1.
The examiner points out that region IV of the LRP contains a proteolytic site
which allows the minireceptor having region IV to be cleaved into an 80 kDa
amino-terminal fragment and an 85 kDa carboxyl-terminal fragment. Answer, page 4.
In detecting expression of the LRP minireceptors in cells transfected with the gene for
the region IV minireceptor, Western blotting indicated the presence of the
protease-cleaved 80 kDa amino-terminal fragment and 85 kDa carboxyl-terminal
fragment, as well as the unprocessed precursor. Id. (citing Willnow, paragraph
spanning pages 15828 and 15829, and Figure 2).
Thus, the examiner urges that claim 1 encompasses the proteolytic processing of
the region IV minireceptor described by Willnow.
Appellants argue that, contrary to claim 1’s requirement that the proteolytic
cleavage release the protein’s carboxyl terminus from the membrane, “Willnow
describes an LRP which is cleaved at an N-terminal, extracellular site, and the protease
does not and cannot release from the membrane any C-terminal tail.” Appeal Brief,
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