Appeal No. 94-3007 Application 07/809,039 . . . [D]ue to the close structural similarity and closeness of relationship of the isomers it is expected that they would possess very close properties . . . . Next, the examiner states (Examiner’s Answer, pages 4-5, bridging paragraph): The compound of claim 30 differs from the compound of the prior art in that the claimed compound is drawn to an anhydrous form of the peptide, as opposed to the prior art hydrated compound. Such difference however would have been obvious to one of ordinary skill in the art at the time the invention was made since the claimed anhydro compound, a transpeptidation reaction intermediate between the parent compound and the claimed isomer, is the sole pathway to the formation of an aspartyl isomer product. (Note the Bodansky [sic, Bodanszky] reference at pp. 336- 338, submitted by appellants.) Also, note the suggested[2] 2 Bodanszky et al. (Bodanszky), “Side Reactions in Peptide Synthesis,” Synthesis 1981, pages 333-338, 351-356 (May 1981), was first cited by applicants in their Information Disclosure Statement filed May 4, 1988 (Paper No. 3). First, we note that the examiner did not mention Bodanszky in the statement of the rejection. See In re Hoch, 428 F.2d 1341, 1342 n.3, 166 USPQ 406, 407 n.3 (CCPA 1970)(“Where a reference is relied on to support a rejection, whether or not in a ‘minor capacity,’ there would appear to be no excuse for not positively including the reference in the statement of the rejection.”) Second, Bodanszky appears to be providing peptide chemists with notice of problem side reactions and undesirable by-products which they must always consider. Bodanszky appears to lead skilled artisans away from the side reactions. Third, while Bodanszky does teach that the Asp residues are susceptible - 10 -Page: Previous 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 NextLast modified: November 3, 2007