Appeal No. 2005-0258 Page 2
Application No. 09/768,877
Claims 51 and 53 are illustrative of the subject matter on appeal and are
reproduced below:
51. A method of screening for a modulator of calpain 10 function
comprising:
a) obtaining an [sic] calpain 10 polypeptide;
b) contacting the calpain 10 polypeptide with a putative modulator;
and
c) assaying for modulation of calpain 10 function by the putative
modulator.
53. The method of claim 51, wherein the calpain 10 polypeptide has a
sequence comprising amino acid 1 to 47 of SEQ ID NO:2[.]
The references relied upon by the examiner are:
Van De Loo et al. (Van de Loo), “An oleate 12-hydroxylase from Ricinus
communis L. is a fatty acyl desaturase homolog,” Proc. Natl. Acad. Sci. USA,
Vol. 92, pp. 6743-6747 (1995)
Meyer et al. (Meyer), “Biologically active monomeric and heterodimeric
recombinant human calpain I produced using the baculovirus expression
system,” Biochem. J., Vol. 314, pp. 511-519 (1996)
Broun et al. (Broun), “Catalytic Plasticity of Fatty Acid Modification Enzymes
Underlying Chemical Diversity of Plant Lipids,” Science, Vol. 282, pp. 1315-1317
(1998)
Witkowski et al. (Witkowski), “Conversion of a ß-Ketoacyl Synthase to a Malonyl
Decarboxylase by Replacement of the Active-Site Cysteine with Glutamine,”
Biochemistry, Vol. 38, pp.11643-11650 (1999)
Bork, “Powers and Pitfalls in Sequence Analysis: The 70% Hurdle,” Genome
Research, Vol. 10, pp. 398-400 (2000)
Seffernick et al. (Seffernick), “Melamine Deaminase and Atrazine
Chlorohydrolase: 98 Percent Identical but Functionally Different,” J. Bacteriol.,
Vol. 183, No. 8, pp. 2405-2410 (2001)
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