Appeal No. 2004-1106 July 2004
Application 09/871,388 Page 4
is said to contain a stretch of 9 amino acid residues that are absolutely conserved with
DKUZ. [Id., p. 22, ll. 15-23.]
6. The bovine MADM (i.e., Mammalian Disintegrin-Metalloprotease) protein
described by Howard comprises a prodomain (i.e., prosequence), metalloprotease and
disintegrin domains, a cysteine-rich domain and finally a transmembrane domain
(Howard, p. 48; Figure 5).
7. Howard also describes isolation of rat and human homologs of MADM (abstract;
Figure 2, p. 48) as well as raising a polyclonal antiserum in rabbits against a peptide
(FDANQPEGKKC) corresponding to amino acids 485-495 of the deduced rat and
human polypeptide sequences (p. 47, c. 2, first full ¶; Figure 2, p. 48).
8. The protease domain of MADM contains an extended zinc binding site,
HEVGHNFGSPH (residues 383-393), identical to that depicted in appellants' Figure 1A
for MKUZ (HEVGNHFGSPH) and substantially identical to that depicted for DKUZ
(HEIGHNFGSPH).6 [Compare appellants' Figure 1A and Howard, p. 48, c. 2, ¶ 2.]
9. According to Howard, MADM had been shown to cleave myelin basic protein
(Howard, p. 45, c. 2, ¶ 1) (see also, appellants' specification, p. 22, ll. 16-17).
10. According to appellants' specification, mutant forms of DKUZ containing either a
point mutation predicted to abolish protease activity or lacking the protease domain
entirely, act in a dominant negative manner in fruit flies, while a truncated form of the
6 According to appellants' specification (p. 4, l. 27 - p. 5, l. 1), "[O]ne or more amino acid residues
within the sequence can be substituted by another amino acid of a similar polarity which acts as a
functional equivalent, resulting in a silent alteration. Conservative substitutes for an amino acid within the
sequence may be selected from other members of the class to which the amino acid belongs. For
example, the nonpolar (hydrophobic) amino acids include alanine, leucine, isoleucine [I], valine [V],
proline, phenylalanine, tryptophan and methionine."
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