Appeal No. 2005-0258 Page 14
Application No. 09/768,877
appellants disclose that calpain 10 “has domains I-to-III” we note, as does the
examiner (Answer, page 8), that several calpain 10 isoforms do not contain
domains I-III. Specifically, with reference to figures 1A-1H, we note that calpains
10c, 10f, 10g and 10h appear to be missing all or part of domain III, and calpains
10f, 10g and 10h appear to be missing part of domain II. Regarding, domain T,
calpains 10b, and 10c-10h appear to be missing all or part of domain T. In
addition, as the examiner explains (Answer, page 8),
while the specification discloses that a calpain 10 protein is similar
in structure to calpain 5 and 6 (page 31, lines 8-11), it does not
provide any guidance as to which … structural elements … are
specific to a calpain 10 and are not found in a calpain 5 or 6 such
that one of skill in the art would know if a polypeptide is a calpain
10 or a calpain 5 or 6.
Accordingly, we are not persuaded by appellants’ assertion (Brief, page 15), “that
calpains are a family of structurally related intracellular multidomain cysteine
proteinases containing a papain-related catalytic domain, whose activity depends
on calcium.” Without a disclosure of the structural characteristics that distinguish
calpain 10 from other members of the calpain family, there is no way to
distinguish calpain 10 from the other members of the calpain family. As the
examiner explains (Answer, page 8),
[t]he specification fails to provide the structures of all the calpain 10
polypeptides required in the claimed method, or the structural
elements which are common to all calpain 10 proteins from any
organism. In addition, the specification fails to disclose which are
the critical structural elements in the human and mouse calpain 10
polypeptides disclosed which are required in any polypeptide to
display calpain 10 activity.
For the foregoing reasons, we disagree with appellants’ assertion (Brief,
page 15), “[g]iven the more than adequate description provided in the
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