Appeal No. 1998-0053
Application 08/444,628
Murphy et al. (Murphy), “Assessment of the role of the fibronectin-like domain of gelatinase
A by analysis of a deletion mutant,” Journal of Biological Chemistry, Vol. 269, No. 9, pp.
6632-6636 (March 4, 1994).
O’Connell et al. (O’Connell), “Analysis of the role of the COOH-terminal domain in the
activation, proteolytic activity, and tissue inhibitor of metalloproteinase interactions of
gelatinase B,” Journal of Biological Chemistry, Vol. 269, No. 21, pp. 14967-14973 (May
27, 1994).
Claims 1 and 4 stand rejected under 35 U.S.C. § 103 as unpatentable over
Goldberg, O’Connell, Murphy and Liotta. Claim 2 stands rejected under 35 U.S.C. § 103
as unpatentable over Goldberg, O’Connell, Murphy, Liotta, Hirel and Thomas. We reverse
both rejections.
BACKGROUND
Matrix metalloproteinases comprise a family of enzymes collectively capable of
degrading all components of extracellular matrix. Members of the family include several
collagenases, a 92 kDa gelatinase, a 72 kDa gelatinase, three stromalysins, macrophage
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metalloelastase, matrilysin, etc. The 92 kDa gelatinase consists of five structural
domains: the amino-terminal and zinc-binding catalytic domains shared by all members of
the secreted metalloproteinase gene family, the collagen binding fibronectin-like domain
shared with the 72 kDa gelatinase, a carboxyl-terminal hemopexin-like domain shared by
all matrix metalloproteinases except matrilysin, and a unique 54 amino acid proline-rich
3The 92 kDa gelatinase is also known in the art as gelatinase B, and as MMP-9;
the 72 kDa gelatinase is also known as gelatinase A, and as MMP-2.
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