Appeal No. 2005-0410
Application No. 09/902,461
immunosuppressant or that instructions are included with the enzyme for
administration.” Id., pp. 5-6. Nevertheless, the examiner contends that
[i]t would have been obvious that the enzyme is a precursor of
recombinant human acid "-glucosidase and that Chinese hamster ovary cells
were used to produce the claimed enzyme since Fuller teaches that the claimed
enzyme can be produced in hamster ovary cells and that the enzyme is a
precursor of recombinant human acid "-glucosidase since such desirable results
are obtained with such an enzyme. . . .
The adjustment of particular conventional working conditions (e.g.,
determining [the] result effective amounts of the enzyme beneficially taught by
the cited references, the interval the enzymes are administered, the method of
administration of the enzyme, etc., especially within the broad ranges instantly
claimed) is deemed merely a matter of judicious selection and routine
optimization which is well within the purview of the skilled artisan [Answer, p. 6].
First, we do not agree with the examiner’s initial premise that Bivjoet discloses
the administration of human acid "-glucosidase to a patient to treat Pompe disease.
Rather, we find that Bivjoet discloses the production of the enzyme in transgenic mice
and its administration to (i) cultured fibroblasts and muscle cells derived from GSD-II
patients; and (ii) GSD-II knock-out mice.
Second, although there is evidence of record which indicates that the human acid
"-glucosidase produced in transgenic mice is not identical to the human acid "-
glucosidase produced in CHO cells [see, Reuser (para. bridging pp. S108-109) attached
as Exhibit C to the Brief;4 see also, the specification, p. 6, lines 8-13], Bijvoet does not
4 Reuser, et al. (Reuser), “Enzyme therapy for Pompe disease: from science to
industrial enterprise,” Eur. J. Pediatr., vol. 161, pp. S106-S111 (2002).
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