Appeal 2007-0746
Application 10/139,496
noted in the Nair paper, when Zajic’s “antigen that is 65-68kDA in size . . .
was sequenced the sequence was homologous to CTL2.” (Answer 5-6.)
Appellants respond:
Zajic et al. teaches use of KHRI-3 antibody in a Western
blotting procedure to identify the presence or absence of
protein on a membrane. Specifically, Zajic et al.'s teaching of
gel purification (i.e., separating by electrophoresis on a gel
matrix by size) of the total population of proteins present
within inner-ear organ of Corti tissue, followed by Western
blotting (i.e., transferring the total population of size
separated proteins present within the gel matrix onto a
membrane and using sequential hybridization of primary
antibody specific for a protein on the gel (e.g., KHRI-3)
followed by a detectable secondary antibody specific for the
primary antibody to detect the presence or absence of a
protein on the membrane) does not provide an
immunopurified protein of the present invention.
(Reply Br. 4-5.)
In view of these positions, we frame this decisive issue: Has the
Examiner made a prima facie case that the glycoprotein isolated and
identified by Zajic is the same glycoprotein as that claimed by Appellants,
when the claim language is given its broadest reasonable interpretation, as
we are required to do during examination?
Findings of Fact Relating to Patentability Under §§ 102(b) and 103(a)
The Examiner found Zajic discloses the same glycoprotein as is
claimed in claim 1 (see Answer 5-6).
Appellants dispute this finding. (Br. 7-12; Reply Br. 4-7.)
Claims 1 and 10 are directed to a product, a “glycoprotein” that is
“reactive with a KHRI-3 monoclonal antibody,” and not a process for
immunopurifying the protein.
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