Appeal No. 2005-0908 Page 7
Application No. 09/261,329
functional properties, predictability of which changes can be tolerated in a
protein’s amino acid sequence and obtain the desired properties/activity requires
a knowledge of guidance with regard to which amino acids in the protein’s
sequence, if any, are tolerant of substitution and which are conserved (i.e.
expectedly intolerant to substitution), and detailed knowledge of the ways in
which the proteins’ structure relates to its function.” Id. at 5-6. But, the examiner
asserts, the disclosure is limited to a single modified cellulase. See id. at 6.
The examiner further argues that “[w]hile recombinant and mutagenesis
techniques are known, it is not routine in the art to screen for multiple
substitutions . . . and the positions within a protein’s sequence where amino acid
substitutions can be made with a reasonable expectation of success in obtaining
the desired activity/utility are limited in any protein and the result of such
substitutions is unpredictable.” Id. (emphasis in original). Moreover, according to
the rejection, the tolerance for substitutions decreases as the number of
substitutions increases. See id.
The rejection concludes:
The specification does not teach a rational and predictable
scheme for substituting any residues in SEQ ID NO:5 with an
expectation of obtaining the endoglucanase function that is
exhibited by a disclosed mutant and the specification provides
insufficient guidance as to which of the essentially infinite possible
choices is likely to be successful.
Therefore, on skilled in the art would require guidance
beyond that provided in the specification as to how to make a
modified cellulase having endoglucanase activity with the amino
acid sequence of an unknown homology to SEQ ID NO:5. Without
such guidance, the experimentation left to those skilled in the art is
undue.
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