Appeal 2007-1159
Application 09/839,946
U.S.C. § 6(b). Claim 50 is representative of the claims on appeal, and reads
as follows:
50. An isolated tetrameric mammalian uricase, wherein at least about 90%
of said uricase is in a tetrameric form and less than about 10% of said
uricase is in a non-tetrameric aggregated form.
The Examiner relies on the following references:
Conley, “Purification of Uricase From Mammalian Tissue,”
Preparative Biochemistry, Vol. 9, pp. 197-203 (1979).
Conley, “Thermodynamics and Stoicheiometry of the Binding of
Substrate Analogues to Uricase,” Biochem. J., vol. 187, pp. 727-732 (1980).
Lee, “Generation of cDNA Probes Directed by Amino Acid Sequence:
Cloning of Urate Oxidase,” Science, vol. 239, pp. 1288-1290 (1988).
We affirm.
DISCUSSION
Claims 50-53 stand rejected under 35 U.S.C. § 102(b) as being
anticipated by Lee. As Appellants do not argue the claims separately, claims
51-53 stand or fall with claim 50, and we thus focus our analysis on claim
50.
According to the Examiner:
Lee [ ] teach[es] the recombinant production of full
length amino acid sequence of porcine Urate oxidase (also
known as uricase) (see abstract lines 8-10) which is tetrameric
and is substantially pure. Mammalian uricase is disclosed as a
tetramer with subunit size of 32,000 daltons (page 1288,
column 2, first paragraph after the abstract). The reference
further teaches purification to homogeneity of Porcine and
murine urate oxidase (see, page 1289, column 2).
(Answer 5 (emphasis in original).)
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