Appeal No. 2001-0733 Page 7
Application No. 09/095,429
on an erroneous scientific theory to support the combination, that is, that
enzymatic activity is sufficient for cytotoxicity. See Appeal Brief, page 5. The
examiner argues, however, that “[t]he roles of the pryroglutamic acid residue in
cytotoxicity and enzymatic activities is truly irrelevant,” and that “one of ordinary
skill in the art would attempt to make a similar protein with similar characteristics
regardless of the role or function of the pyroglutamyl residue.” Examiner’s
Answer, page 29. The rejection fails, however, whether it is based on the
function of the pyroglutamic acid, or whether it is based on making a similar
protein with similar characteristics. We will address both of these rationales in
turn.
With respect to the function of the pyroglutamic acid, the rejection asserts
that because the pyroglutamic acid residue aids in forming the active site, “any
onconase missing [that] important amino acid[ ] is expected to have
compromised enzymatic and the associated cytotoxic activity.” Thus, the
rationale underlying the rejection appears to be that one would be motivated to
place the ATG start codon, which encodes methionine, at the -1 position, and
also mutate the methionine at position 23 to another amino acid, in order to allow
for cyanogen bromide cleavage of the recombinant protein at the methionine at
the -1 position, and thus allowing spontaneous cyclization of the glutamine
residue at position 1 to the pyroglutamic acid residue. The examiner also argues
that the Ardelt reference supports the theory that enzymatic activity is required
for cytotoxic activity, and that appellants have not provided any experimental
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