Appeal No. 1997-0483
Application No. 07/648,900
polypeptide of amino acid residues 407 to 486 binds thrombin, thereby inhibiting its
clotting activity, without increasing protein C activation (see p. 4, penultimate para.; p. 6,
para. 2; p. 7, para. 4; p. 9, para. 5; pp. 20--22, Examples 14-16; p. 25, para. 2).
Thus, we interpret the polypeptides of the claimed invention as encompassing
polypeptides which identically correspond to residues 407 to 486 of a mammalian
thrombomodulin as shown in Figure 6 as well as "similar" sequences having modifications
both within the sequence, e.g., conservative substitutions at non-identical amino acid
residues as suggested in specification Example 13, and additional substituents adjacent
to the termini of the sequence, e.g., cross-linking groups suitable for attaching the
polypeptide to a surface, and non-glycosylated derivatives thereof with the proviso that the
sequence must be capable of binding to thrombin, thereby inhibiting its clotting activity,
without affecting, i.e., increasing, protein C activation. We do not interpret claim 5 as
reciting a polypeptide including additional amino acid residues up to and including
residues 234 to 286, residues 310 to 486, or even the entire protein because such
polypeptides significantly increase protein C activation (see e.g., specification, p. 4, para.
5
5).
5In the brief (pp. 18-19, § b.), appellants state:
The specification provides the amino acid sequences of thrombomodulin from several
species and describes which regions, and residues within regions, are conserved. It is
readily apparent to one skilled in the art that if the protein contains substitutions for an
amino acid residue but is still biologically active, that the substituted amino acid is not
essential for activity. Moreover, applicants have shown that not only are the claimed
peptides active, but that longer fragments including other amino acids, up to and including
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