Appeal No. 1997-2517
Application No. 08/155,102
mutated a/native ß heterodimer would not act as an antagonist for native a/ß
hormone unless it bound to its receptor. Therefore, the argument goes, those
skilled in the art would not have expected the a subunits encoded by the instantly
claimed DNA to be useful as antagonists, nor did the prior art suggest any other
use for the mutant a subunits encoded by the claimed DNA. Thus, Appellants
conclude, the prior art fails to provide motivation to make the claimed DNA.
The examiner appears to accept Appellants’ position that those skilled in
the art would have expected a gonadotropin hormone comprising an a subunit
mutated at amino acids 88-92 to be unable to bind its receptor. However, the
examiner argues that this expectation would not have led to the conclusion that
the a subunits encoded by the claimed DNA would be useless as antagonists.
The examiner argues that
the modified a-subunit still binds the ß-subunit and competes with
the unmodified a-subunit for the ß-subunit, i.e., it is an antagonist.
When the modified a -subunit (as for example where one or more of
residues 88-92 is removed . . .) is bound to the ß-subunit, the a/ß
dimer is inactive (or at least less active) and is an antagonist of the
unmodified a-subunit for the ß-subunit.
Examiner’s Answer, page 15. Thus, the examiner’s position is that those skilled
in the art would have expected that an a subunit having a mutation in amino
acids 88-92 would function as an antagonist because, even though a/ß
heterodimers comprising such a mutant would not bind to the hormone receptor,
the mutant a subunit would compete with native a subunit for binding to the ß
subunit and thereby reduce the amount of active a/ß heterodimer.
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