Ex Parte Ballance et al

Patent Trial and Appeal Board

May 12, 2017

13855434 (P.T.A.B. May. 12, 2017)

United States Patent and Trademark Office
UNITED STATES DEPARTMENT OF COMMERCE
United States Patent and Trademark Office
Address: COMMISSIONER FOR PATENTS
P.O.Box 1450
Alexandria, Virginia 22313-1450
www.uspto.gov
APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO.
13/855,434 04/02/2013 David J. Ballance 06478.1575-01000 5979
22852 7590 05/16/2017
FINNEGAN, HENDERSON, FARABOW, GARRETT & DUNNER
LLP
901 NEW YORK AVENUE, NW
WASHINGTON, DC 20001-4413
EXAMINER
ROBINSON, HOPE A
ART UNIT PAPER NUMBER
1652
NOTIFICATION DATE DELIVERY MODE
05/16/2017 ELECTRONIC
Please find below and/or attached an Office communication concerning this application or proceeding.
The time period for reply, if any, is set in the attached communication.
Notice of the Office communication was sent electronically on above-indicated "Notification Date" to the
following e-mail address(es):
regional-desk @ finnegan. com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte DAVID J. BALLANCE and DARRELL SLEEP1
Appeal 2016-003294
Application 13/855,434
Technology Center 1600
Before JEFFREY N. FREDMAN, TIMOTHY G. MAJORS, and
DEVON ZASTROW NEWMAN, Administrative Patent Judges.
MAJORS, Administrative Patent Judge.
DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134 involving claims to methods
of treating a patient by administering an albumin fusion protein comprising a
Factor IX polypeptide. The claims have been rejected as obvious. We have
jurisdiction under 35 U.S.C. § 6(b).
We REVERSE.
STATEMENT OF THE CASE
Appellants’ “invention relates generally to Therapeutic proteins
(including, but not limited to, a polypeptide, antibody, or peptide, or
1 Appellants identify the Real Party in Interest as NOVOZYMES
BIOPHARMA DK A/S. (App. Br. 3.)
Appeal 2016-003294
Application 13/855,434
fragments and variants thereof) fused to albumin or fragments or variants of
albumin.” (Spec. 1:12—13.)2 According to the Specification, such fusion
proteins “exhibit extended shelf-life and/or extended or therapeutic activity
in solution.” (Id. at 1:16—17.)
Claims 61 and 63—73 are on appeal. Claim 61 is illustrative:
61. A method of treating a patient in need of a Factor IX
polypeptide, comprising the step of administering an effective
amount of an albumin fusion protein comprising a Factor IX
polypeptide fused to an albumin polypeptide, wherein the
albumin polypeptide has the ability to prolong the serum half-life
of the fused Factor IX polypeptide compared to the unfused
Factor IX polypeptide, wherein the fused Factor IX polypeptide
has Factor IX coagulant activity, wherein the Factor IX
polypeptide is fused at the N-terminus of the albumin
polypeptide, and wherein the albumin polypeptide is selected
from:
a) a full-length albumin;
b) a mature albumin;
c) a fragment of albumin;
d) a polypeptide consisting of an amino acid sequence
at least 95% identical to SEQ ID NO: 18; and
e) amino acids 1 to 387 of SEQ ID NO: 18;
and wherein the Factor IX polypeptide is selected from:
i) a full-length Factor IX;
ii) an activated Factor IX (Factor IXa);
iii) a fragment of a Factor IX having a deletion that
consists of 1-50 amino acid residues as compared to
the sequence of amino acids 1 (Tyr) to 416 (Thr) of
SEQ ID NO:46;
iv) a polypeptide consisting of an amino acid sequence
at least 90% identical to the sequence of amino acids
1 (Tyr) to 416 (Thr) of SEQ ID NO: 46; and
2 References to the Specification (“Spec.”) herein refer to Appellants’
substitute Specification dated Sept. 16, 2013.
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Application 13/855,434
v) a mature Factor IX.
(App. Br. (Claims App’x 1).)
The claims stand rejected under 35 U.S.C. § 103(a) over Ballance,3
Schulte,4 Fleer,5 and Axelrod.6 (Ans. 3.)
Appellants identify the following pending appeals as related:
1) U.S. Application No. 11/927,600 (Appeal No. 2016-003160);
2) U.S. Application No. 13/855,454 (Appeal No. 2016-003295); and
3) U.S. Application No. 11/927,602 (Appeal No. 2016-005026).
(See App. Br. 3.)
DISCUSSION
Issue
The Examiner rejected claims 61 and 63—73 as obvious over Ballance
(as evidenced by Schulte), Fleer, and Axelrod. (Ans. 3.) The Examiner
finds that “Ballance et al. teach fusion proteins comprising human serum
albumin (protein of 585 amino acids) and human growth hormone . . . [and]
that the albumin fusion protein extends the half-life in the circulation of the
fusion partner protein compared to an unfused state.” (Id. at 3.) According
to the Examiner, Ballance also teaches “the fusion protein comprises a
fragment that may be the N-terminal portion or C-terminal portion.” (Id. at
3 Ballance, WO 97/24445, published July 10, 1997.
4 Schulte, Half-life extension through albumin fusion technologies, 124
Thrombosis Research, Suppl. 2 S6-8 (2009).
5 Fleer et al., US 5,876,969, issued Mar. 2, 1999.
6 Axelrod et al., Phenotypic correction of factor IXdeficiency in skin
fibroblasts of hemophilic dogs, 87 Proc. Natl. Acad. Sci. 5173—77 (1990).
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3— 4.) The Examiner finds that Schulte “disclose[s] that treatment of
hemophilia B requires frequent infusions of Factor IX to ameliorate bleeding
episodes, therefore, FIX therapy is one such treatment modality that could
benefit from [] an albumin fusion protein to prolong the half-life and reduce
dosing.” (Id. at 4.)
The Examiner finds that Ballance “does not expressly teach the
stabilization of Factor IX (i.e. prolonging the half-life) or a method of
treating a patient in need of Factor IX,” and thus turns to Fleer. (Id. at 4.)
According to the Examiner, “Fleer teach[es] albumin fusion proteins with a
number of therapeutic proteins and state[s] that albumin can be fused to
coagulation factors ... for the purposes of prolonging the half-life.” (Id. at
4— 5.) The Examiner further finds “Fleer et al. also teach single and double
fusion proteins with albumin (see the entire patent and claim 1).” (Id. at 5.)
The Examiner finds “[t]he art generally recognizes that FIX is a
coagulation factor.” (Id.) The Examiner also finds “Axelrod et al. teach the
structure of Factor IX and fragments thereof including [various] deletions.”
(Id.)
The Examiner concludes the claimed method of administering a FIX
albumin fusion protein would have been obvious. (Id.) According to the
Examiner, “Schulte demonstrates the need in the art for extension of FIX as
a therapeutic for Hemophilia B via a fusion molecule such as albumin.”
(Id.) The Examiner reasons the skilled artisan “would be motivated to
modify the conjugate taught by Ballance et al. by replacing the growth
hormone with a FIX . . . based on the disclosure in the art of the function of
albumin as prolonging the half-life of other proteins in circulation and the
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fact that there is a strong need in the art to help short lived proteins for
therapy to have a prolonged half-life.” (Id. at 5—6.) Further, the Examiner
reasons, the skilled person “would [] have a reasonable expectation of
success . . . because of the examples of albumin fused to a therapeutic
protein provided by Ballance et al. and Fleer et al.” (Id. at 6.)
Appellants argue the Examiner’s combination of prior art fails to
render the claims obvious. Appellants contend Fleer’s disclosure of “a
genus of albumin fusion proteins containing a coagulation factor does not
render obvious the claimed species of a Factor IX-albumin fusion protein.”
(App. Br. 6—9.) Appellants further contend that, at the time of the invention,
the skilled artisan “would not have predicted that albumin fusion would
‘prolong the serum half-life of the fused Factor IX polypeptide’ as claimed.”
(Id. at 6, 9—19.) Appellants argue the skilled person “would not have
predicted the orientation-dependent coagulant activity of the claimed Factor
IX-albumin fusion proteins” and more specifically “Appellant’s unexpected
discovery that Factor IX retains biological activity only when fused to the
amino-terminal [N-terminal] end of albumin.” (Id. at 6, 19—24.) Appellants
contend “based on the teachings of Ballance and Fleer, one skilled in the art
likely would have predicted the exact opposite of Appellant’s discovery
regarding orientation-dependence” (id. at 26) and that “the cited prior art
teaches away from the claimed N-terminal albumin fusion proteins” (id. at
28). (See also Id. at 26—29.)
In support of its arguments concerning the patentability of the claims
on appeal, Appellants cite to, among other things, multiple declarations from
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skilled persons and publications in the scientific literature. We discuss
Appellants’ evidence further below. (App. Br. passim.)
The issue on appeal is whether the preponderance of the evidence of
record supports the Examiner’s conclusion of obviousness.
Findings of Fact (FF)
The Examiner’s findings of fact and statement of the rejection are
provided at pages 3—6 of the Examiner’s Answer and pages 6—10 of the
August 18, 2014 Final Rejection. (See also Ans. 11—33 (Response to
Argument); Final Act. 11—20 (Response to Arguments); Adv. Act. 2—11.)7
FF 1. Ballance teaches “fusion of a molecule of albumin, or variants
or fragments thereof, to a molecule of growth hormone or variants or
fragments thereof, the fusion proteins having an increased circulatory half-
life over unfused growth hormone.” (Ballance 3:27—30.)
FF 2. Ballance teaches:
Preferably, the fusion protein comprises HA [human albumin],
or a variant or fragment thereof, as the N-terminal portion, with
hGH [human growth hormone] or a variant or fragment thereof
as the C-terminal portion [i.e., hGH is fused to the C-terminal
end of the albumin], so as to minimise any possible negative
effects on receptor binding. Alternatively, a fusion protein
comprising HA, or a variant or fragment thereof, as the C-
terminal portion, with hGH or a variant or fragment thereof as
the N-terminal portion, may also be capable of signal
transduction. Generally, the polypeptide has only one HA-
derived region and one GH-derived region.
7 In the Advisory Action dated Dec. 23, 2014 and the Final Rejection dated
Aug. 18, 2014, the Examiner cites to Hallahan et al., US 5,969,040, issued
Oct. 19, 1999 (“Hallahan”), but as the Examiner does not cite to or appear to
rely on Hallahan in the Examiner’s Answer, we do not consider it here.
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(Mat 4:3-11.)
FF 3. Fleer teaches “[biologically active polypeptides comprising a
therapeutically active polypeptide fused to human serum albumin or a
natural variant thereof.” (Fleer Abstract.) Fleer further teaches “albumin
variants designate any protein with a high plasma half-life which is obtained
by modification.” {Id. at 1:23—25.)
FF 4. Fleer teaches
the polypeptide having a therapeutic activity is a polypeptide of
human origin or a molecular variant. For example, this may be
all or part of an enzyme, an enzyme inhibitor, an antigen, an
antibody, a hormone, a factor involved in the control of
coagulation, an interferon, a cytokine ... of a growth factor
and/or of differentiation [and for example the transformant
growth factors (TGFs), the blood cell differentiation factors
(erythropoietin, M-CSF, G-CSF, GM-CSF and the like), insulin
and the growth factors resembling it (IGFs), or alternatively cell
permeability factors (VPF/VEGF), and the like] ... of a
cytostatic factor (and for example the proteins which bind to
galactosides), of a plasma (and for example von Willebrand
factor, fibrinogen and the like)....
{Id. at 2:22-49 (brackets in original) (emphases added).)
FF 5. Fleer teaches
The active part of the molecules of the invention can be
coupled either directly or via an artificial peptide to albumin.
Furthermore, it may constitute the N-terminal end as well as the
C-terminal end of the molecule. Preferably, in molecules of the
invention, the active part constitutes the C-terminal part of the
chimera [i.e., polypeptide fused to C-terminal of albumin],
{Id. at 3:28-33.)
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Principles of Law
“The combination of familiar elements according to known methods
is likely to be obvious when it does no more than yield predictable results.”
KSRInt’l Co. v. Teleflex Inc., 550 U.S. 398, 416 (2007).
Prima facie obviousness may be rebutted with evidence of secondary
considerations and when such evidence is submitted, all of the evidence is
considered anew. In re Piasecki, 745 F.2d 1468, 1472—73 (Fed. Cir. 1984).
Secondary considerations include, inter alia, long-felt but unsolved needs,
failure of others, and unexpected results. In re Rouffet, 149 F.3d 1350, 1355
(Fed. Cir. 1998).
Analysis
Claim 61
Looking to the Examiner’s findings and reasoning concerning the
combination of Ballance (as evidenced by Schulte), Fleer, and Axelrod
alone, we agree that claim 61 would have been prima facie obvious.8 But
considering the totality of the evidence of record, we reach a different
conclusion. Although Fleer teaches albumin fusions and suggests use with
factors involved in coagulation, coagulation factors encompass dozens of
8 Appellants point out that “Schulte was published in 2009, about 9 years
after the filing date of the instant application . . . [and] cannot be used to
show that one of ordinary skill in the art had motivation and a reasonable
expectation of success in generating the claimed Factor IX-albumin fusion
proteins at the relevant time.” (App. Br. 5.) The Examiner responds that
Schulte is an appropriate “evidentiary reference.” (Ans. 11.) Appellants
have the better position. The Examiner is relying on Schulte for its
substantive teaching as “a source of motivation for increasing the half-life of
FIX.” (Reply Br. 4 n. 2.) We do not rely upon Schulte.
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potential polypeptides. (App. Br. 7.) Also, the functionally closest peptide
tested in Fleer, von Willebrand factor, which can reasonably be
characterized as a coagulation factor, did not exhibit coagulant activity as
required by the claims. {Id. at 8—9.) As we discuss in greater detail below,
Appellants have provided persuasive and countervailing objective evidence
of nonobviousness. When this evidence is considered along with the
teachings of the applied prior art, the decision tilts in Appellants’ favor.
Appellants emphasize that, in mentioning “a factor involved in the
control of coagulation,” Fleer discloses a broad genus “compris[ing] many
functionally and structurally distinct polypeptides.” (App. Br. 7 (citing
Tanaka9).) Appellants also point out that, in the lone example in which
Fleer tested fusion proteins comprising a coagulation factor —fragments of
vWF — that these fusion constructs “inhibit the physiological function of
vWF, not [] enhance its normal coagulant activity as contemplated by the
instant invention.” {Id. at 9.)
The fact that coagulation factors have diverse structures and functions
does not, in itself, persuade us that the Examiner’s reliance on Fleer is
flawed. To the contrary, as the Examiner noted, “Fleer provides a myriad of
therapeutic proteins as potential fusion partners which demonstrates that
different protein structures with different functions can be fused to albumin.”
(Ans. 15.) Put differently, in expressly reciting polypeptides with quite
different structures and functions (e.g., EPO versus vWF), Fleer suggests the
design of active therapeutic fusion constructs despite the diversity. That
9 Tanaka et al., Blood Coagulation: Hemostasis and Thrombin Regulation,
108:5 Anesthesia & Analgesia 1433^46 (2009).
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said, Appellants’ contention that the vWF-fusion constructs exemplified in
Fleer inhibit coagulant activity — opposite from vWF’s normal activity and
what is claimed — weakens somewhat the notion that an ordinarily skilled
person would have a reasonable expectation of success in designing a FIX
fusion protein with coagulant activity as claimed. (App. Br. 9.)
Appellants argue the prior art, and especially Ballance and Fleer, must
be viewed through the lens of “background knowledge in the art.” (App. Br.
11.) This knowledge, Appellants contend, is that “the circulatory half-life of
a polypeptide depended on its molecular size due to much faster renal
clearance of small polypeptides from the blood plasma.” {Id. at 9.)
According to Appellants’ declarant, Dr. Sleep,10 it was known in the art that
“plasma clearance of proteins decreased rapidly with increasing molecular
size from about 20 kD to about 60-70 kD . . . [and] a size of 60-70 kD or
above showed only very little or almost no renal clearance.” (Sleep Decl.
14.) It “was also known in the art that the serum half-life of a small protein,
such as human growth hormone (hGH), could be increased by expressing it
as a genetic fusion with human serum albumin (HSA), which is a large (67
kD) protein.” {Id. at | 5.) Dr. Sleep declares “Factor IX is a much larger
molecule, having a molecular size of about 57 kD.” {Id. at 17.) Dr. Sleep
further declares that “at the priority date of [the present application] it was
thought in the art that FIX was too large for clearance from circulation via
the kidneys. . . . Thomsen et al. taught regarding the related blood clotting
10 Declaration of Dr. Darrell Sleep dated May 12, 2014 (“Sleep Decl.”) Dr.
Sleep cites a number of publications in support of his opinions. We omit
citation to most of those references here for brevity.
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Factor VII that ‘the 50 kDa glycoprotein FVIIa molecule is a low clearance
compound.’” {Id.)11 Thus, Dr. Sleep opines, “one skilled in the art would
have thought that Factor IX, as the related Factor VII, is already large
enough to be excluded from renal secretion, and therefore would not have
expected that fusing Factor IX to albumin would prolong the circulatory
half-lives of this factor to any useful extent.” {Id.)
When viewed in this historical context, Appellants contend, this
explains why the working examples in Ballance and Fleer fused albumin to
smaller polypeptides or fragments, with the largest having a molecular
weight of about 27 kD. (App. Br. 14.) According to Appellants, “nothing in
Ballance and Fleer provided any reasonable expectation that albumin fusion
would increase the half-life of substantially larger polypeptides, such as
Factor IX.” {Id. at 15.)
Here again, this evidence and argument alone from Appellants does
not persuade us the Examiner erred in concluding that claim 61 would have
been obvious. Fleer teaches that “albumin variants designate any protein
with a high plasma half-life which is obtained by modification” (FF 3) and,
in expressly teaching the fused polypeptide may be “all or part of an enzyme
[etc.],” Fleer suggests its constructs are not limited to fusions with fragments
or small molecules. (FF 4.) Also, as the Examiner notes, Fleer identifies a
number of polypeptides that have somewhat larger molecular weights (e.g.,
EPO). (Ans. 12—13.) Moreover, while FVII may have been recognized as a
11 See Thomsen et al., Pharmacokinetics of Recombinant Factor Vila in the
Rate A Comparison of Bio-, Immuno- and Isotope Assays, 70:3
Thrombosis and Haemostasis 458-64 (1993).
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low clearance compound based on size (approx. 50 kD), FIX (approx.
57 kD) is below the renal permeability threshold (60—70 kD) reported in the
art and Dr. Sleep’s declaration. (See, e.g., Sleep Deck 4, 7.)
Accordingly, by fusing to albumin, some increase in circulatory half-life —
even if minor — would have reasonably been expected. Nevertheless,
Appellants’ evidence does at least suggest the skilled person at the time of
the invention would not have expected that fusing FIX to albumin would
have necessarily resulted in a substantial increase in half-life.
Appellants next cite to data concerning orientation dependency and
unexpected results when Factor IX is fused to the N-terminal end of
albumin. (App. Br. 19—24.) According to Appellants, testing provided by
Dr. Thomas Weimer12 shows the criticality of FIX fusions at the N-terminus:
“the activity-to-antigen ratio of the N-terminal fusion protein (protein 980) is
more than 50-fold larger than that of the C-terminal fusion protein (protein
2397.)” (Id. at 21 (citing Weimer Deck 17).) In contrast, “the activity-to-
antigen ratio approaches zero for the fusion protein with Factor IX fused
[only] at the C-terminal end of albumin.” (Id.) Also citing Dr. Weimer’s
testing, Appellants point out that double fusions (fusing FIX to both the C-
and N-terminal ends of albumin) provide a protein with significant activity
compared to fusion constructs at the C-terminal end only, which “is virtually
inactive.” (Id. (citing Weimer Deck 7—11.) According to Appellants (and
Dr. Weimer), “both Ballance and Fleer teach that therapeutic polypeptides
are preferably fused at the C-terminal end of albumin, which is opposite to
12 See Declaration of Dr. Thomas Weimer dated August 23, 2013 (“Weimer
Deck”).
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the orientation recited in the claims on appeal.” (Id. at 26; see also Weimer
Decl. 114.)
Appellants’ data concerning the claimed N-terminal fusions provides
persuasive objective evidence of nonobviousness. The Examiner’s response
relies heavily on the prima facie case, and the teachings in both Ballance and
Fleer that polypeptides may be fused to the N- or C- terminal end of
albumin. (Ans. 22—27.)13 The Examiner has not, however, provided
persuasive evidence or scientific reasoning explaining why the results
Appellants produced would have been expected.14 Indeed, as Appellants
contend, the prior art suggests the opposite — that optimal activity would
have been observed when a polypeptide is fused at the C-terminal end of
albumin. (Reply Br. 13—15; FF 2, 5.) Although we do not limit the prior art
to its preferred embodiments, here the evidence unexpectedly shows that,
had the skilled artisan modified the prior art to include FIX fused to the C-
terminus, the result would have been a virtually inactive protein.
We recognize, but are not persuaded by, the Examiner’s emphasis in
the Response to Argument, that Fleer claims a double-fusion construct.
(See, e.g., Ans. 23—26.) On the record here, the mention of double fusions in
Fleer’s claims is not entitled to any talismanic importance without an
13 At points throughout the Examiner’s response, the Examiner appears to
mistakenly cite to evidence submitted in Appellants’ related appeals. (See,
e.g, Ans. 26 (discussing data in a September 2013 declaration of Dr.
Weimer).)
14 The Examiner asserts that Drs. Weimer and Sleep appear to contradict
each other (Ans. 22), and that Appellants have provided other
“contradictory” statements (id. at 25). For the reasons given by Appellants,
we are unpersuaded there is any discrepancy. (Reply Br. 11—12, 14—15.)
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accompanying disclosure teaching or suggesting a particular advantage of
such a construct. Fleer, as does Ballance, clearly prefers fusions at the C-
terminal end of the albumin, and suggests those fusion proteins provide
optimal therapeutic activity. (FF 2, 5.) The Examiner, however, asserts that
the skilled person “could conclude that because Fleer claims a double fusion
in claim 1 after making single fusions at both terminus that they were aware
that the double fusion produced the highest activity.” (Ans. 23.) This is
speculation. And, in any event, when obviousness is at issue the question is
not what the skilled person could have concluded or done, but what they
reasonably would have done. See Belden Inc. v. Berk-TekLLC, 805 F.3d
1064,1073 (Fed. Cir. 2015).
The Examiner also responds that “there is a high expectation of
success, because Ballance and Fleer made albumin fusion proteins
comprising therapeutic proteins that are C-terminally or N-terminally
oriented and Fleer also made a fusion that was N and C terminally oriented.”
(Ans. 25.) We are not persuaded. Fusions with Factor IX having any of
these orientations were not made. And, as noted by Appellants and Dr.
Weimer, neither Ballance nor Fleer discloses any in vivo therapeutic activity
when a polypeptide is fused to the N-terminal end of albumin, while such
activity is disclosed for C-terminal fusions. (See Weimer Decl. Tflf 13—16.)15
Inasmuch as the Examiner invokes an inherency rationale (Ans. 25, 29) to
produce a FIX polypeptide with the claimed “coagulant activity” when fused
15 Ballance discloses that in vitro testing showed that fusions of hGH to the
N-terminal end of albumin were “significantly less potent” than fusions at
the C-terminal end. (See Ballance 22:4—7; see also Weimer Decl. 116.)
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at the N-terminal, we are unpersuaded. See Par Pharma., Inc. v. Twi
Pharms., Inc., 773 F.3d 1186, 1195—96 (Fed. Cir. 2014) (holding that a
“high standard” must be met “to rely on inherency to establish the existence
of a claim limitation in the prior art in an obviousness analysis.”) This is
especially so when the “natural result” of the combination of Ballance and
Fleer would have been a fusion at the C-terminal end of albumin, yet
Appellants’ data shows the FIX polypeptide is unexpectedly inactive unless
there is a fusion at the N-terminus. Id. at 1196.
When the Examiner’sprima facie case is considered anew, in light of
all the evidence of record, we are unpersuaded that claim 61 would have
been obvious over Ballance (as evidenced by Schulte), Fleer, and Axelrod.
Appellants have provided persuasive argument and objective evidence of
nonobviousness that rebuts the Examiner’s evidence of obviousness. Mintz
v. Dietz & Watson, Inc., 679 F.3d 1372, 1379 (Fed. Cir. 2012)
(“Obviousness requires . . . walking] a tightrope blindfolded (to avoid
hindsight)—an enterprise best pursued with the safety net of objective
evidence.”) This is not a case where the prima facie case is so strong that it
controls the obviousness determination. See Pfizer, Inc. v. Apotex, Inc., 480
F.3d 1348, 1372 (Fed. Cir. 2007). We thus reverse the rejection of claim 61
and its dependent claims. In reFritch, 972 F.2d 1260, 1266 (Fed. Cir. 1992)
(“[Dependent claims are nonobvious if the independent claims from which
they depend are nonobvious.”)
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Conclusion of Law
We conclude the preponderance of the evidence of record does not
support the Examiner’s conclusion that claims 61 and 63—73 would have
been obvious.
SUMMARY
We reverse the rejection of claims 61 and 63—73 under U.S.C.
§ 103(a) over Ballance, Schulte, Fleer, and Axelrod.
REVERSED
16