Appeal No. 1997-0094
Application No. 08/188,232
would have had a reasonable expectation of success of obtaining an active thymosin
peptide by amidating the C-terminal of a thymosin " and/or thymosin " analog given the
1 11
factual basis for appellant's above argument, i.e., the markedly decreased
immunoreactivity of the amidated peptides of Ishimura. In short, the examiner has not
explained why one of ordinary skill in the art would have amidated Gly-29 as claimed.
The examiner further states that "Zatz discloses amidation of the thymosin family
irrespective of whether the compound belongs to the alpha or beta thymosin group"
(answer, p. 8). However, the examiner has not pointed out, and we do not find, where Zatz
addresses the issue of how amidating the C-terminal of a thymosin peptide affects its
biological activity. At best, Zatz merely suggests the existence of an amide composition
3
for thymosin ß (caption beneath Fig. 2, p. 265).
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Thus, we find the examiner has not carried her burden of establishing a prima facie
case of obviousness and has relied on impermissible hindsight in making her
determination of obviousness. In re Fritch, 972 F.2d 1260, 1266, 23 USPQ2d 1780, 1784
(Fed. Cir. 1992). Having concluded that the examiner has not established a prima facie
case of obviousness, we do not reach the rebuttal evidence in the Raitzer
3According to Table I (p. 267), thymosin ß per se has no reported biological activity.
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