Appeal No. 1997-2364
Application 08/137,086
used, also taking into account the subsequent stage of separation between the
phosphopeptide aggregates and non phosphorylated peptides, said separation being
effected . . . by an ultrafiltration step.” Moreover, Brule cautions that “due attention should
also be paid especially to the cut off threshold of the ultrafiltration membrane, so as to
avoid passage of the phosphopeptidic aggregate through this membrane” (column 6, line
67, through column 7, line 14, emphasis added).
Although “each of the above ultrafiltration steps may be followed by a diafiltration
step during which there is added, continuously or discontinuously, a liquid such as water or
aqueous salt-containing solution, with a view to further purify the ultrafiltration products,”
there is no indication that maintaining the concentration of the bivalent cation will affect the
end result. Indeed, Brule indicates that “water proved to be suitable for diafiltration.”
Column 7, lines 30-36. Regardless, it is clear that the casein hydrolysate is separated into
two fractions by Brule’s method: “on the one hand, as a permeate, non phosphorylated
peptides, and on the other, as a retentate, phosphopeptides” (column 7, lines 45-47). This
is in contrast to the claimed invention wherein one fraction contains selected
phosphopeptides, and the other contains a mixture of other phosphopeptides and non-
phosphorylated peptides.
Thus, we see no basis for the examiner’s assertion that Brule anticipates the
claimed invention, even in its broadest aspect. Nor do we see any basis for concluding
that it would have been obvious to adjust the concentration of the bivalent cation and/or the
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