Appeal No. 2004-1106 July 2004
Application 09/871,388 Page 9
disclosed for distinguishing between the prior art bovine MADM and the disclosed KUZ
polypeptides. Nowhere, does Appellant have written support for an antibody that can
specifically bind to SEQ ID NOS 2, 4, 6 and 8 and not MADM" (Answer, p. 4). Further
according to the examiner, "the term specifically binds in the antibody art does not
remove prior art antibodies from reading upon the claimed invention because of art
recognized properties of antibody cross reactivity" (id., p. 5).
In other words, we understand the examiner's position to be two-fold. First, the
recited KUZ proteins are necessarily distinguishable from bovine MADM based upon
their respective enzymatic activity, i.e., KUZ catalyzes cleavage of NOTCH proteins,
while MADM catalyzes cleavage of myelin basic protein (FF 4, 9 and 10). Second, a
KUZ-specific antibody reads on cross-reactive antibodies, e.g., the MADM antiserum
raised against a peptide (FDANQPEGKKC) corresponding to amino acids 485-495 of
the deduced rat and human polypeptide sequences described by Howard (FF 7).
Therefore, a KUZ-specific antibody does not necessarily, i.e., inherently, fail to bind
specifically with MADM.
D. Discussion
Appellants' specification clearly indicates that KUZ binding specificity may be
determined, at least, on the basis of (1) protease activity, (2) equilibrium binding
constants, (3) ability to function as negative mutants and (4) ability to raise antibody,
e.g., antiserum, in a heterologous host, e.g., a rabbit (FF 22). In other words, there is
more than one reasonable construction of "KUZ binding specificity." Thus, the binding
specificity that distinguishes the recited KUZ proteins from bovine MADM is not
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