Appeal No. 2005-1171
Application No. 09/469,485
exceeds that of the pure protein” [footnotes omitted]. Valenzuela II, p. 349, col. 1, first
complete para. Valenzuela II still further discloses that the yeast-produced 22-nm
HBsAg particles are “immunoreactive with anti-HBsAg antibodies” and that they “are
similar to those made by human carrier patients or by a hepatoma cell line.” Id., para
bridging pp. 349-350. Valenzuela II concludes that “[t]he similarity in structure of the
yeast particle to bona fide 22-nm particles and the high immunogenicity in animals
emphasize the possible value of the HBsAg particle as a vaccine.” Id., p. 350, col. 2,
lines 3-5. Given this disclosure of the highly immunogenic nature of the yeast-produced
rHBsAg particles and their possible use as a vaccine, we find no suggestion in
Valenzuela II to modify the rHBsAg described therein in any manner. To the contrary,
we find that the reference “teaches away” from any further modifications of rHBsAg.
We recognize that the examiner relied on Builder as the primary reference.
However, we find that Builder is directed to the problems associated with expressing
heterologous proteins in E. coli; viz., the recovery of heterologous proteins which are
often “precipitated within the cell as ‘refractile’ bodies” in an inactive form. Builder, col.
1, lines 9-16. The appellants point out, and the examiner does not disagree, that the
proteins in the refractile bodies disclosed by Builder are insoluble. See, e.g., the
abstract; col. 2, lines 15-22; col. 12, lines 39-41. Builder further discloses that “drastic
means is [sic, are] required to bring this protein into solution so that it can be used.” Id.,
col. 2, lines 59-61. This is accomplished by using a strong denaturing solution which
unfolds the protein and dissolves it into the [denaturing] solution. Id., col. 2, lines 61-62;
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