Appeal No. 2005-0258 Page 13
Application No. 09/768,877
product. See for example Figure 1H, where the polypeptide labeled
calpain 10[h] lacks all the domains present in calpain 10[a] which
correlate with the proteolytic activity associated with calpains and
only contains domain I and domain T (C-terminal domain).
Regarding the calpain 10 domains, appellants assert (Brief, page 14),
figure 5 provides “an alignment of calpain 10 and various calpains indicating the
domains.” Further, appellants assert (Brief, bridging sentence, pages 14-15), “a
structural description of the domains of calpain 10, such as the specific
calmodulin-like Ca2+ binding domain” is disclosed on page 31 of the specification.
At page 31 of their specification, appellants disclose that
[c]alpain 10 diapain[5] is an atypical calpain and is similar in
structural organization to the other atypical calpains, calpain 5 and
calpain 6, in that it has domains I-to-III, lacks the calmodulin-like
Ca2+-binding domain and has a divergent C-terminal domain,
domain T…. Calpains 5, 6 and 10 define a distinct subfamily (FIG.
6).
Accordingly, notwithstanding appellants’ assertion to the contrary, calpain 10
does not contain a calmodulin-like Ca2+ binding domain. In addition, while
5 According to appellants’ specification (page 29), “[c]alpain 10 is a ‘diapain’ that has been
identified by the present invention.” With regard to the term “diapain”, appellants’ explain
(specification, page 33), “[s]ince it is a variant in the calpain 10 gene that is associated with
diabetes, the inventors suggest that the protein encoded by this gene be called diapain-1
(diabetes calpain). As such the terms ‘calpain 10’ and diapain-1 are used interchangeably
herein.” Accordingly, we note that the genus encompassed by the term “calpain 10” as it is used
in the method of claim 18 also reads on variants associated with the calpain gene that are
associated with diabetes.
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