Appeal No. 1997-0094
Application No. 08/188,232
Glu-21, Glu-27 and Asn-28" (p. 705, c. 2). Immunoreactivity decreased by about 40-fold if
either Asn-28 or its terminal OH group was replaced by -NH and by about 500-fold if the
2
COOH-terminal dipeptide Glu-Asn was replaced by -NH or Glu-27 was replaced by Ala
2
(p. 705, c. 1).
Zatz describes the amino acid sequences of "-thymosins, including thymosin " ,
1
des (25-28) " , " and prothymosin " (Fig. 1), and of ß-thymosins (Fig. 2) (p. 265).1 11
According to the examiner, it would have been obvious to delete "one amino acid
residue from the known 1-30 peptide fragment especially since the peptide activity is
known to reside in the N-terminus fragment of 1-28 residues", i.e., in thymosin " (answer,
1
p. 6).
First, we note that the examiner has incorrectly defined the 1-30 amino acid residue
fragment as thymosin " (see answer, p. 3, "thymosin alpha (1-30)"). Thymosin " is11 11 11
the peptide defined by residues 1-35 of the N-terminal of prothymosin ". Second, even
assuming arguendo that it would have been obvious to add one more amino acid residue
to thymosin " or to shorten the 30 amino acid residue thymosin " analog of Akibo I by1 11
one amino acid residue to obtain an active peptide, the examiner has not explained why
one of ordinary skill in the art would have amidated the
C-terminal amino acid, Gly-29.
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