Appeal No. 2004-1106 July 2004
Application 09/871,388 Page 10
necessarily antibody-based. Rather, as the examiner found, the recited KUZ proteins
may be distinguished from bovine MADM based upon their respective enzymatic
activities, i.e., MADM cleaves myelin basic protein, whereas KUZ cleaves NOTCH
proteins (FF 4, 9 and 10), a substrate-based distinction. Consequently, while KUZ
binding specificity may be antibody-based for example, as argued by appellants (Brief,
p. 2; Reply, p. 2), antibody binding is not the only reasonable construction of a KUZ
specific binding which necessarily distinguishes the preferred KUZ polypeptides of SEQ
ID NOS 2, 4, 6 and 8 from the bovine MADM protein of Howard.
Appellants have narrowed their claimed invention to a composition of antibody or
antibody fragments which differentiates between homologous proteins found in three
specific species, i.e., Drosophila KUZ (SEQ ID NO. 2), human KUZ (SEQ ID NOs 4 and
6) and mouse KUZ (SEQ ID NO. 8), from that found in a fourth specific species, i.e.,
bovine MADM. However, the primary amino acid sequence of bovine MADM is 95%
identical with the primary amino acid sequence of mouse KUZ as defined by SEQ ID
NO. 8 (FF 5). Therefore, given the high amino acid sequence identity between MADM
and MKUZ, especially in view of the MADM antiserum described by Howard raised
against a common peptide sequence, it does not follow that the only reasonable
construction of a KUZ specific binding antibody is an antibody that necessarily would
not specifically bind to MADM.
Based on the foregoing, the decision of the examiner to reject claims 14-21 and
23-33 for lack of original descriptive support is affirmed.
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