Appeal No. 2006-0484 Page 6
Application No. 09/657,729
Appellant also argues that Higgins “describes a method for electrochemical
assisted biosynthesis and has nothing to do with analytical studies or determinations.
. . . [T]he claimed step of ‘analyzing the sam[pl]e using a detection scheme . . .’ is not
found in Higgins.” Appeal Brief, page 7. That is, “[t]he analyses or ‘detection means’
employed by Higgins are performed only in support of verifying and studying the
heterogeneous electron transfer reaction between the enzyme and the electrode. . . .
[T]he application is bioelectrochemical synthesis which has nothing to do with the
proposed invention. No mention is made of poising the electrode at various potentials
. . . and using an independent detection means (sensitive to the extent of interaction
between target and sample) in order to study the potential or redox dependence of
interactions between a sample and target species.” Id.
As we understand it, Appellant’s argument is that Higgins’ method does not
anticipate the claims because the redox environment of the sample is controlled in
Higgins for the purpose of generating reducing equivalents to enhance the activity of the
luciferase enzyme, and in the claimed method the redox environment is controlled in
order to determine whether it affects the interaction of a target and a sample. We do
not agree that the difference, if any, between the purpose of Higgins' experiment and
that of Appellant’s disclosed method distinguishes claims 1 and 51 from the prior art.
Luciferase-mediated light production depends on interaction between several
components: luciferase, decyl aldehyde, molecular oxygen (O2), and a source of
reducing equivalents (NADH normally, free electrons in Higgins’ system). See Higgins,
col. 6, lines 39-42 and 55-56. Thus, Higgins’ detection of the light that results from the
action of luciferase on its substrate (decyl aldehyde) in the presence of other reactants
Page: Previous 1 2 3 4 5 6 7 8 9 10 11 12 Next
Last modified: November 3, 2007