Appeal No. 96-0051 Page 7
Application No. 07/987,256
$-ketoacyl-ACP synthase proteins (Paper No. 1 at 8). A person
skilled in the art, upon reading in the specification that
The ACP column removes several proteins including a major
contaminant which also showed a molecular weight at about
50 kD[]
would have understood that the contaminant was so designated because
it lacked synthase activity. Consequently, the examiner’s concern
about the 50 kD contaminant is not supported by the preponderance of
evidence of record.
Appellants contend that there is only one disclosed 50 kD
protein with synthase activity (Paper No. 30 (App. Br.) at 15).
According to the specification, a 50 kD synthase protein elutes in
two fractions. The first fraction primarily has synthase II
activity; the second, primarily synthase I activity. The
specification indicates that two-dimensional gel analysis of the
50 kD protein band with synthase II activity produces “at least two
spots” (Paper No. 1 at 23-24). The specification does not explain
these two spots. It continues by explaining that the 50 kD proteins
with synthase I and synthase II activities appear to be closely
related (Paper No. 1 at 24). From that point on, the specification
refers to “the 50 kD protein” as though only one 50 kD protein is
relevant.
Claim 21 requires an enabling disclosure for a cDNA encoding a
50 kD Ricinus communis $-ketoacyl-ACP synthase protein. The
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