Appeal No. 2002-0872 Page 3
Application No. 08/470,849
In addition, the examiner finds (Answer, page 5), “[c]laims 20-23 are directed to human
tumor necrosis factor receptor immunoglobulin chimeric protein isolated from the
process of claims 18-19 which results in specific glycosylation properties.” According to
the examiner (id.), “[t]hese glycosylation limitations of molar ratios of sialic acid and N-
acetylglucosamine are inherent properties of the glycosylated [sic] of human tumor
necrosis factor receptor immunoglobulin chimeric protein and the protein of Ashkenazi
et al. can reasonably be considered to be same [sic] absent any evidence to the
contrary.”
However, as appellants point out (Brief, page 4, emphasis removed), “Ashkenazi
et al. do not disclose the specific culturing conditions used; such as the temperature at
which the cells are grown and/or held in a production phase, the osmolality of the
media, or the sodium butyrate concentrations of the media.” Appellants emphasize
(Brief, pages 5-6), “that when the cell culture process is altered by the use of separate
growth and production phases, and when alterations are made in the production phase
of cell culture, variation in the oligosaccharide component of an expressed glycoprotein
will result.” In support of this argument appellants rely on Goochee (U.S. Patent No.
5,510,261), and Tables I-V of their specification.
In response, the examiner argues (Answer, page 6), “no evidnece [sic] has been
presented that the claimed genus of human tumor necrosis factor receptor
immunoglobulin chimeric protein is glycosylated differently in CHO cells versus the HEK
293 cells. Furthermore, the claims are directed to product[-]by[-]process or range
limitations of the glycosylation and not a specific species.
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