Appeal No. 2004-1369 Page 4
Application No. 08/966,233
In this regard, we note that appellant discloses (specification, page 20),
“GDF-1 is most homologous to VG-1 (52% and least homologous to inhibin-α
(22%) and the TGF-β’s (26-30%).” However, as the examiner points out
(Answer, page 21), despite appellant’s emphasis on the structural similarity of
GDF-1 to members of the TGF-β superfamily, the similarity accounts for less
than half of the GDF-1 protein. In other words, only about 107 of GDF-1’s 357
amino acids share similarity with TGF-β. While GDF-1 is disclosed by appellant
to be least homologous to the TGF-β superfamily appellant discloses
(specification, page 12),
The TGF-β superfamily encompasses a group of proteins
affecting a wide range of differentiation processes. The structural
homology between GDF-1 and the known members of the TGF-β
superfamily and the pattern of expression [of] GDF-1 during
embryogenesis indicate that GDF-1 is a new member of this family
of growth and differentiation factors. Based on the known
properties of the other members of the [sic] this superfamily, GDF-1
can be expected to possess biological properties of diagnostic
and/or therapeutic benefit in a clinical setting.
However, as set forth in the specification (page 14), “[a] determination of the
specific clinical settings in which GDF-1 will be used as a diagnostic or as a
therapeutic tool await further characterization of the expression patterns and
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