Appeal No. 2005-1171 Application No. 09/469,485 disulfide bonds within the protein, we find that Valenzuela I discloses that the sequences flanking a hydrophobic region are rich in both proline and cysteine residues. Valenzuela I, p. 817, col. 1, lines 12-15. Valenzuela I suggests that “the abundant cysteine residues could make intra- and intermolecular linkages to form the surface coat of the virus.” Id., lines 17-19. However, we find no teachings with respect to the expression of the HBsAg gene. Therefore, it reasonably follows that Valenzuela I does not describe the immunogenicity of the cloned HBsAg (rHBsAg) or the role of disulfide bonds with respect to the integrity of the antigen. Accordingly, since the examiner is clearly relying on a reference which is not before us, the rejection is summarily reversed. Be that as it may, we neverthless searched the application file and found, of record,1 another Nature publication by Valenzuela (Nature, vol. 298, pp. 347-350 (1982)(hereinafter Valenzuela II), which has the page numbers referred to in the examiner’s rejection. Assuming, arguendo, that we were to consider this publication in the manner proposed by the examiner, we still could not affirm the rejection. Valenzuela II discloses the production of 22-nm surface antigen particles resulting from the expression of DNA encoding HBsAg in yeast. Valenzuela II further discloses that “[t]he predominant form of HBsAg produced by human cells is the so-called 22-nm particle. Its biophysical properties are well documented and its immunological potency 1 See, “List of References cited by applicant and considered by the examiner,” entered May 5, 2003. 5Page: Previous 1 2 3 4 5 6 7 8 9 NextLast modified: November 3, 2007