Appeal No. 2006-1035 Page 4
Application No. 09/925,140
• Lin,4 as teaching that “[r]emoval of the amino terminal histidine of glucagon
substantially decreases the ability of the molecule to . . . activate adenylate
cyclase.”
Id.
The examiner concluded that
one skill[ed] in the art would realize that a sequence that is 90% identical
to SEQ ID NO:1 would not necessarily have the activity of SEQ ID NO:1
and therefore would not function as SEQ ID NO:1. . . . In view of the lack
of predictability in the art, lack of guidance, and lack of examples, one
skilled in the art would be forced into undue experimentation in order to
practice the broadly claimed invention.
Id., page 6.
Appellants have presented no evidence or reasoning to rebut the examiner’s
position that many of the species encompassed by part (b) of claim 3 are likely to lack
the function ascribed in the specification to SDHH. Rather, Appellants argue that the
claimed polynucleotides are useful even if they encode inactive polypeptides: “[T]he
claims are to polynucleotides, not the polypeptides they encode, and therefore it is the
use of the polynucleotides that is relevant. . . . The specification recites many instances
where a polynucleotide may be used, . . . whether or not th[e] encoded polypeptides
had enzymatic activity.” Appeal Brief, page 5.
Appellants argue that the claimed polynucleotides can be used “in assays to
detect the presence of metabolism disorders or cancer,” (id.), “to detect and quantitate
gene expression in biopsied tissues in which expression of SDHH may be correlated
with disease” (id.), as probes for detecting related sequences (id., page 6), in
4 Lin et al., “Structure-function relationships in glucagon: Properties of highly purified des-His1, monoiodo-,
and [des-Asn28, Thr29](homoserine lactone27)-glucagon,” Biochemistry, Vol. 14, pp. 1559-1563 (1975)
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