Appeal No. 2005-0410 Application No. 09/902,461 report any differences. To the contrary, Bivjoet discloses that the recombinant enzyme produced in milk (transgenic mice) and CHO cells had similar activity in both in vitro and in vivo assays. Bijvoet, p. 1819, col. 2, last sentence; p. 1822, col. 1, paras. 3-4. Thus, Bijvoet concludes that Altogether, the production of recombinant human acid "-glucosidase in the mammary gland of transgenic animals seems a good alternative to production by CHO cells because of lower intrinsic costs and similar therapeutic potential. Guided by these positive results, we have started large-scale production of recombinant acid "-glucosidase in the milk of transgenic rabbits [emphasis added] [Bivjoet, p. 1822, col. 1, para.5]. We do not find that given these teachings, one of ordinary skill in the art would have been motivated to employ the human acid "-glucosidase taught by Fuller (i.e., the enzyme produced in CHO cells). To the contrary, we find that Bijvoet would have, at best, suggested the use of the recombinant enzyme produced in transgenic mice to treat GSD-II patients. On this record, the only suggestion we find to pursue claimed methods of treating GSD-II patients using the enzyme produced in CHO cells and administering said enzyme “periodically at adminstrative intervals” is in the appellant’s disclosure. Thus, we find that the examiner has engaged in impermissible hindsight to arrive at the conclusion that the claimed invention would have been obvious over Bijvoet and Fuller. In re Fritch, 972 F.2d 1260, 1266, 23 USPQ2d 1780, 1784 (Fed. Cir. 1992); Interconnect Planning Corp. v. Feil, 774 F.2d 1132, 1138, 227 USPQ 543, 547 (Fed. Cir. 1985); W.L. Gore & Assocs. v. Garlock, Inc., 721 F.2d 1540, 1553, 220 USPQ 303, 312-313 (Fed. Cir. 1983) cert. denied 469 U.S. 851 (1984)(“To imbue one of ordinary 13Page: Previous 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 NextLast modified: November 3, 2007