Appeal No. 2002-0091 Page 2 Application No. 08/479,884 from the N-terminus of 191-amino acid human growth hormone, wherein said variant is not hGH-V. The examiner does not rely on any references. All of the pending claims stand rejected under 35 U.S.C. § 112, first paragraph, as nonenabled. We reverse. Background “Human growth hormone (hGH) . . . exhibits a multitude of biological effects including linear growth (somatogenesis), lactation, activation of macrophages, insulin-like effects and diabetagenic effects.” Specification, page 5. “The three- dimensional structure of hGH is not available.” Id., page 6. Attempts have been made to map the receptor-binding site in hGH using either peptide fragments or monoclonal antibodies, but these techniques have not produced acceptable results. See id., pages 6-7. The specification discloses a method for identifying active domains in proteins by systematically replacing amino acid residues of the wild-type protein to create protein variants, and comparing the activity of the variants to that of the wild-type protein. See, e.g., pages 13-14. The method is exemplified with hGH, among other proteins. See pages 44-57. The specification provides numerous exemplary hGH variants,1 most having an amino acid substitution in a single position. See, e.g., pages 76-79. Other 1 Appellants put the number at “over 150”, page 6 of the Appeal Brief, which the examiner does not dispute. Not all of these embodiments are encompassed by claim 88, however.Page: Previous 1 2 3 4 5 6 7 8 9 10 NextLast modified: November 3, 2007