Appeal No. 2001-0733 Page 7 Application No. 09/095,429 on an erroneous scientific theory to support the combination, that is, that enzymatic activity is sufficient for cytotoxicity. See Appeal Brief, page 5. The examiner argues, however, that “[t]he roles of the pryroglutamic acid residue in cytotoxicity and enzymatic activities is truly irrelevant,” and that “one of ordinary skill in the art would attempt to make a similar protein with similar characteristics regardless of the role or function of the pyroglutamyl residue.” Examiner’s Answer, page 29. The rejection fails, however, whether it is based on the function of the pyroglutamic acid, or whether it is based on making a similar protein with similar characteristics. We will address both of these rationales in turn. With respect to the function of the pyroglutamic acid, the rejection asserts that because the pyroglutamic acid residue aids in forming the active site, “any onconase missing [that] important amino acid[ ] is expected to have compromised enzymatic and the associated cytotoxic activity.” Thus, the rationale underlying the rejection appears to be that one would be motivated to place the ATG start codon, which encodes methionine, at the -1 position, and also mutate the methionine at position 23 to another amino acid, in order to allow for cyanogen bromide cleavage of the recombinant protein at the methionine at the -1 position, and thus allowing spontaneous cyclization of the glutamine residue at position 1 to the pyroglutamic acid residue. The examiner also argues that the Ardelt reference supports the theory that enzymatic activity is required for cytotoxic activity, and that appellants have not provided any experimentalPage: Previous 1 2 3 4 5 6 7 8 9 10 11 12 NextLast modified: November 3, 2007