Appeal No. 1997-2140
Application 08/357,820
3. The cDNA sequence which encodes the truncated mutant, SEQ ID NO:1, of the
92 kDa gelatinase having an amino acid sequence as shown in FIG. 2 consisting of
residues 106-216 fused to residues 391-443 of the parent molecule.
4. The cDNA which encodes the truncated mutant of the 92 kDa gelatinase of claim
3 containing an additional Met-Gly residue at the N-terminus.
The references relied on by the examiner are:
Goldberg et al. (Goldberg) 4,992,537 Feb. 12, 1991
Liotta et al. (Liotta) 5,270,447 Dec. 14, 1993
Hirel et al. (Hirel), “Extent of N-terminal methionine excision from Escherichia coli proteins
is governed by the side-chain length of the penultimate amino acid,” Proc. Natl. Acad. Sci.
USA, Vol. 86, pp. 8247-8251 (November 1989).
Thomas et al. (Thomas), “Expression in Escherichia coli and characterization of the heat-
stable inhibitor of the cAMP-dependent protein kinase,” Journal of Biological Chemistry,
Vol. 266, No. 17, pp. 10906-10911 (June 15, 1991).
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).
Claim 3 stands rejected under 35 U.S.C. § 103 as unpatentable over Goldberg,
O’Connell, Murphy and Liotta. Claim 4 stands rejected under 35 U.S.C. § 103 as
unpatentable over Goldberg, O’Connell, Murphy, Liotta, Hirel and Thomas. We reverse
both rejections.
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