Appeal No. 2002-1479 Page 2
Application No. 08/794,042
Appellant relies on the following references:
Light et al. (Light & Janska), “The amino-terminal sequence of the catalytic
subunit of bovine enterokinase,” Journal of Protein Chemistry, Vol. 10, No. 5, pp.
475-480 (1991)
LaVallie et al. (LaVallie), “Cloning and functional expression of a cDNA encoding
the catalytic subunit of bovine enterokinase,” Journal of Biological Chemistry,
Vol. 268, No. 31, pp. 23311-23317 (1993)
Fonseca et al. (Fonseca), “The purification and characterization of bovine
enterokinase from membrane fragments in the duodenal mucosal fluid,” Journal
of Biological Chemistry, Vol. 256, No. 23, pp. 14516-14520 (1983)
Liepnieks et al. (Liepnieks), “The preparation and properties of bovine
enterokinase,” Journal of Biological Chemistry, Vol. 254, No. 5, pp. 1677-1683
(1979)
Claim 42 stands rejected under 35 U.S.C. § 102(b) as anticipated by Light.
We reverse.
Background
Enterokinase is a naturally occurring protease. See the specification,
page 2. The specification discloses that “although extensive research efforts
have been mounted by several different research groups since the first partial
purification of bovine enterokinase more than 15 years ago, no one has yet been
successful in cloning enterokinase. . . . [Bovine enterokinase was] isolated in the
late 1970s. Liepnieks et al., J. Biol. Chem. 254 :1677(1979) described an
enterokinase having 35% carbohydrate, a molecular weight of 150,000, with a
heavy (115,000) and light (35,000) chain connected by one or more disulfide
bonds. Subsequent studies of the light chain, i.e., the catalytic subunit, were
reported in Light et al., J. Biol. Chem. 259:13195(1984). Most recently,
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