Appeal No. 2002-1630 Page 14
Application No. 09/175,713
derived from any of the enumerated chemokines by any kind of alteration. Thus,
the claim encompasses any conceivable mutant or variant of any of the recited
forty-nine chemokines, modified at the amino terminus, provided the modified
chemokine displays chemotactic activity (i.e., it is still a chemokine).
The evidence of record also supports the examiner’s position that the
effect of changing a chemokine’s amino acid sequence is unpredictable. The
examiner cited Proudfoot as evidence that the addition of a methionine residue at
the amino terminus has opposite effects on different chemokines. That is, the
specification shows that the addition of an amino-terminal methionine increases
the activity of the chemokine SDF-1β, while Proudfoot shows that the same
modification to the chemokine RANTES produces an inactive antagonist. See
the Examiner’s Answer, pages 12-13.
In addition, as the examiner noted, the working examples are limited to
SDF-1α and SDF-1β, modified at the amino terminus with either a methionine or
a GroHEK peptide. See the specification, pages 42-52. No working examples
are provided showing the effect of aminooxypentane modification, nor are
examples provided for any of the forty-seven other chemokines recited in claim 5,
nor are examples provided showing the effect of modifying the sequence of a
naturally occurring chemokine. The specification provides no guidance regarding
which direction experimentation should proceed in making and using amino-
terminal-modified chemokines differing from the naturally occurring chemokine
“by any kind of alteration, addition, insertion, deletion, mutation, substitution,
replacement, or other modification.”
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