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.Page: Previous 1 2 3 4 5 6 7 8 9 NextLast modified: November 3, 2007