Appeal No. 2001-1378
Application No. 08/832,571
or a combination of both coding sequences (p110 and p85) on the same construct.
Answer, page 6, Paper No. 9, page 6, Brief, page 18. For reasons similar to those
indicated above, the examiner cites Kapeller, Varticovski and Aronheim as evidence of
knowledge in the art that localization of PI 3-kinase to the plasma membrane is
expected to increase the PI 3-kinase activity, since it brings the enzyme into closer
contact with its substrates, and methods for localizing proteins to membranes by
addition of myristoylation, farnesylation and palmitoylation signal sequences.
. Appellants argue that the examiner has failed to set forth a prima facie case of
obviousness. Brief, page 22. Appellants argue that (Brief, page 19):
At the time of the invention, one of ordinary skill in the art would not
equate the in vivo coexpression of PI 3-kinase subunits, which assumes
conformation that allows them to specifically bind to one another, with that
which occurs “when two subunits are coexpressed [end to end] as a fusion
protein.”
We agree with the appellants that the cited art fails to provide the requisite
expectation of success to establish a prima facie case of obviousness. According to
appellants, Klippel 94 teach that association in vitro of the two subunits produced
separately did not produce an active enzyme, teaching away from an expectation that
the claimed fusion construct would produce active enzyme. Id. In addition, Klippel 93
teach that “a change in the phosphorylation state of the [p110 and p85] subunits [of PI
3-kinase] after association with activated receptor molecules may induce conformational
change and thereby modulate PI 3-kinase activity.” Id. Furthermore, appellants argue
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