Appeal No. 1997-0094
Application No. 08/188,232
Akibo I uses the D-form of the C-terminal amino acid residue Arg-30 to impart
resistance to enzymatic degradation while retaining biological activity. Akibo I does not
disclose or suggest amidating the C-terminal Arg-30 in either D- or L-form. Haritos does
not disclose or suggest amidation.
According to the examiner, "Ishimura is employed for the teaching of amidating the
C-terminus of the thymosin alpha family" (answer, p. 8). However Ishimura suggests that
amidating the C-terminus region of a thymosin " fragment markedly decreases
1
immunoreactivity (p. 705, c. 1). Indeed, appellant argues that "[a]s is known in the art,
changes in the peptide which detrimentally affect binding to antibodies [i.e.,
immunoreactivity] are likely to similarly affect binding to receptors and thus affect
bioactivity" (brief, p. 11). In response, the examiner calls appellant's argument "mere[ly]
speculative without factual basis" (answer, p. 9) and argues that if any binding activity was
present "even to a small extent, [it] would suffice the finding of obviousness" (supplemental
answer, p. 3). We disagree.
Establishing a prima facie case of obviousness requires both some suggestion or
motivation to modify the reference or combine reference teachings and a reasonable
expectation of success. In re Vaeck, 947 F.2d 488, 493, 20 USPQ2d 1438, 1442 (Fed.
Cir. 1991). Here, the examiner has not established that one of ordinary skill in the art
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