Appeal No. 2003-1794 Page 15
Application No. 09/804,969
increased in some tumor cells (Marchisio et al., Exhibit F); expression of
a phospholipase A isozyme increases with prostate tumor grade (Graff
et al., Exhibit F), and a different isozyme of phospholipase A is the
closest genetic marker to a putative glioma tumor suppressor gene
(Hartmann et al., Exhibit F);
• infection by L. monocytogenes results in activation of phospholipase C
and phospholipase D in macrophages (Goldfine et al., Exhibit G); an
isozyme of phospholipase A has anti-bacterial activity (Moreau et al. and
Beers et al., Exhibit G); and an isozyme of phospholipase C is required
for infection of human cells by Ehrlichia chaffeensis (Lin et al., Exhibit
G); and
• an isozyme of phospholipase A is involved in inflammation (Xu et al. and
Springer, Exhibit H).
Thus, these exhibits confirm the specification’s statement that phospholipases
are involved in a variety of different physiological processes. However, neither
the specification nor any other evidence of record indicates which, if any, of the
activities of the various known phospholipases is shared by the polypeptide of
SEQ ID NO:15.
Thus, although the evidence supports Appellants’ position that some
phospholipases are involved in development, and some phospholipases are
involved in various diseases, there is no evidence that all phospholipases are
involved in any of these processes, or that the polypeptide of SEQ ID NO:15 is
involved in any of them. Thus, the evidence shows that, to a person of skill in the
art, the mere identification of the polypeptide of SEQ ID NO:15 as a
phospholipase would not have suggested any specific patentable utility. We
therefore reject Appellants’ argument that § 101 is satisfied by the sequence
similarity of the polypeptide of SEQ ID NO:15 to known phospholipases.
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