Ex Parte Aoki et al

Patent Trial and Appeal Board

Jun 20, 2016

10933723 (P.T.A.B. Jun. 20, 2016)

UNITED STA TES p A TENT AND TRADEMARK OFFICE
APPLICATION NO. FILING DATE
10/933,723 0910212004
51957 7590 06/22/2016
ALLERGAN, INC
2525 DUPONT DRIVE, T2-7H
IRVINE, CA 92612-1599
FIRST NAMED INVENTOR
K. Roger Aoki
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
ATTORNEY DOCKET NO. CONFIRMATION NO.
16952CON4 (BOT) 4933
EXAMINER
GUPTA, ANISH
ART UNIT PAPER NUMBER
IPLA
NOTIFICATION DATE DELIVERY MODE
06/22/2016 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):
patents_ip@allergan.com
pair_allergan@firsttofile.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte K. ROGER AOKI, MICHAEL W. GRA YSTON, and
STEVEN R. CARLSON1
Appeal2013-006105
Application 10/933, 723
Technology Center 1600
Before JEFFREY N. FREDMAN, ULRIKE W. JENKS, and
RY ANH. FLAX Administrative Patent Judges.
JENKS, Administrative Patent Judge.
DECISION ON APPEAL
This is an appeal2 under 35 U.S.C. § 134 involving claims to a method
of treatment using a composition containing a single or dichain neurotoxic
component. The Examiner rejects the claims under the provision of
nonstatutory obviousness-type double patenting. We have jurisdiction under
35 U.S.C. § 6(b). We affirm.
1 According to Appellants, the Real Party in Interest is Allergan, Inc. (App.
Br. 1.)
2 This Appeal is related to Appeals 2013-002207, 2013-002211, 2013-
002212, 2013-002213, 2013-002214, 2013-006027, 2013-006098 and
Ex parte Aoki, 2011 WL 5080231 (BPAI 2011), affd 562 Fed. Appx. 976
(mem.) (Fed. Cir. 2014) (Rule 36).
Appeal2013-006105
Application 10/933,723
STATEMENT OF THE CASE
Background
"Botulinmn toxins, in particular Botulinmn toxin type A, has been
used in the treatment of a number of neuromuscular disorders and
conditions" (Spec. 1: 20-23). "[S]even immunologically distinct
[Botulinum] neurotoxins have been identified. These have been given the
designations A, B, C, D, E, F and G" (id. at 2: 27-29). "Botulinum toxin
type A, the toxin type generally utilized in treating neuromuscular
conditions, is currently available commercially from several sources" (id. at
3: 5-14).
Claims
Claims 1, 21, 22, and 31-39 are on appeal, and can be found in the
Claims Appendix of the Appeal Brief. Claim 1 is representative of the
claims on appeal, and reads as follows:
1. A method for reducing excessive sweating, wherein said
method is a human medical application and comprises the step
of administering to a human patient with excessive sweating a
therapeutically effective amount of a single or dichain form of
the neurotoxic component of a botulinum toxin to thereby
reduce the human patient's excessive sweating, wherein the
neurotoxic component administered to the human patent has a
molecular weight of about 150 kilodaltons.
(App. Br. 22 (Claims Appendix)).
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Issues
The Examiner rejects the claims as follows:
I. claims 1, 21, 22, and 31-39 under the judicially created doctrine of
nonstatutory obviousness-type double patenting over Aoki '886 3 in
view of Tse4 and Simpson5 (Final Act. 3--4);
II. claims 1, 21, 22, and 31-39 under the judicially created doctrine of
nonstatutory obviousness-type double patenting over Aoki '0496 in
view of Tse and Simpson (Final Act. 5-6); and
III. claims 1, 21, 22, and 31-39 under the judicially created doctrine of
nonstatutory obviousness-type double patenting over Aoki '5787 in
view of Tse and Simpson (Final Act. 6-7).
Because the same issue is dispositive for all three rejections we
consider them together.
The Examiner finds that Aoki '886, Aoki '049, and Aoki '578 each
teach the step of administering botulinum toxin for the purpose of alleviating
sweating (Final Act 3 ("administering to cholinergic neurons ... botulinum
toxin ... wherein the autonomic nerve function ... contributes to at least
one symptom of excessive sweating"), Final Act. 5 ("injecting an
3 Aoki et al., US 6,896,886 B2, issued May 24, 2005 (hereinafter "Aoki
'886").
4 Chun. K. Tse et al., Preparation and Characterisation of Homogeneous
Neurotoxin Type A from Clostridium botulinum, 122 EUR. J. BIOCHEM 493-
500 (1982) (hereinafter "Tse").
5 Lance L. Simpson, The Origin, Structure, and Pharmacological Activity of
Botulinum Toxin, 33 PHARMACOL. REV. 155-188 (1981).
6 Aoki et al., US 6,683,049 Bl, issued Jan. 27, 2004(hereinafter "Aoki
'049").
7 Aoki et al., US 6,974,578 Bl, issued Dec. 13, 2005 (hereinafter "Aoki
'578").
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Application 10/933,723
excessively secreting, cholinergically influenced gland, or to the local area
of the gland, with a botulinmn toxin in order to reduce an excessive
secretory activity of the gland"), Final Act. 7 ("administering to the patient
an effective amount of Botulinum toxin in order to reduce the secretion,
wherein the secretion is sweat")), but do not teach the use "the use of the
150 kDa neurotoxin component and the exact dosage claimed" (Final Act. 3,
5, and 7).
However, the Examiner finds that Tse teaches that the neurotoxic
component of type A botulinum "specifically and characteristically inhibited
stimulated and spontaneous release of acetylcholine at the vertebrate
neuromuscular junction" (Final Act. 4, 5, 7) in the same manner as the
complexed toxin, and also, "when injected into the hind leg muscle of a rat,
produced local paralysis within 24 hours" (Final Act. 3--4, 5, 5). Simpson
teaches that the toxin "blocks the release of acetylcholine from cholinergic
nerve endings" and explains that there are seven forms A, B, C, D, E, F and
G that are "synthesized as a single chain polypeptide with a MW of 140,000
to 160,000" (Final Act. 4, 5---6, 7).
The Examiner concludes that the ordinary artisan would have found it
obvious to use the pure toxin of Tse for treatment of excessive sweating
claimed by the US patent because "Tse teaches that pure toxin has similar
activity in the paralysis of muscles as complexed neurotoxin and has similar
activity against spontaneous release of acetylcholine" and Simpson provides
similar teaching (Final Act. 4, 6, 7). The Examiner finds "a reasonable
expectation of success because both the pure toxin and the complexed toxin
have similar activity against spontaneous release of acetylcholine" (Final
Act. 4, 6, 7).
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Findings of Fact
We adopt the Examiner's findings of fact and reasoning regarding the
scope and content of the prior art (see Final Act 3-8; Ans. 4--9). For
emphasis only we highlight the following:
FPL Claims 1-6 of Aoki '886 recite:
1. A method for the control of autonomic nerve function in a
mammal comprising locally administering to cholinergic neurons of
the autonomic system of the mammal an amount ofbotulinum toxin
sufficient to cause denervation of the neurons, wherein said
denervation results in control of autonomic nerve function in a target
tissue or organ innervated by said neurons, wherein the autonomic
nerve function includes the function of an autonomic nerve which
contributes to at least one symptom of excessive sweating.
2. A method according to claim 1 for alleviating excessive
sweating, comprising administering a therapeutically effective amount
of botulinum toxin to the skin of a human.
3. A method according to claim 2, wherein the botulinum toxin
is administered by intradermal injection.
4. A method according to claim 1, wherein the botulinum toxin
is at least one ofbotulinum toxins A, B, C, D, E, For G.
5. A method according to claim 4, wherein the botulinum toxin
is botulinum toxin A.
6. A method according to claim 4, wherein the botulinum toxin
is botulinum toxin D.
FF2. Claims 1-6 of Aoki '049 recite:
1. A method for treating an excessively secreting,
cholinergically influenced gland, the method comprising the step of
injecting an excessively secreting, cholinergically influenced gland, or
to the local area of the gland, with a botulinum toxin in order to
reduce an excessive secretory activity of the gland, wherein the gland
is a sweat gland.
2. The method of claim 1, wherein the botulinum toxin is
botulinum toxin type A.
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Application 10/933,723
3. The method of claim 1, wherein the botulinum toxin is
selected from the group consisting of botulinum toxin types A, B, C,
D, E, F andG.
4. The method of claim 1, wherein the botulinum toxin is
administered in an amount ofbetween 0.01 units and 500 units.
5. The method of claim 1, wherein the botulinum toxin is
administered in an amount ofbetween 0.01 unit and 50 units.
6. A method for treating an excessively secreting,
cholinergically influenced gland, the method comprising the step of
injecting an excessively secreting, cholinergic influenced gland or
local gland area of a human patient with a therapeutically effective
amount of botulinum toxin type A thereby reducing the excessive
glandular secretion, wherein the gland is a sweat gland.
FF3. Claims 1-6 of Aoki '578 recite:
1. A method of treating a secretion of a patient, the method
comprising the step of administering to the patient an effective
amount of Botulinum toxin in order to reduce the secretion, wherein
the secretion is sweat.
2. The method of claim 1, wherein the secretion is a cholinergic
influenced secretion.
3. The method of claim 1, wherein the botulinum toxin is
botulinum toxin type A.
4. A method for treating a cholinergic influenced sweat
secretion of a human patient, the method comprising the step of
administering to a human patient a therapeutically effective amount of
botulinum toxin type A in order to reduce the sweat secretion.
5. A method for treating a gland, the method comprising the
step of administering to a gland a botulinum toxin thereby reducing a
secretory activity of the gland, wherein the gland is a sweat gland.
6. The method of claim 5, wherein the gland is an excessively
secreting sweat gland.
FF4. Tse teaches "the large-scale culture of the C. botulinum (type A).
Isolation of toxin complexes and efficient purification of the
neurotoxin to homogeneity by affinity and ion-exchange
chromatography." (Tse 493).
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FF5. Tse teaches the isolation of heamagglutinin-neurotoxin complexes,
describes removal of the immunogenic haemagglutinin component of
the type A haemagglutinin-neurotoxin complex, and characterization
of the isolated, purified 150 kD neurotoxic component (Tse 493, col.
2; 494, cols. 1-2; 496, col. 2; 499, col. 2).
FF6. Tse teaches that "[t]he purified neurotoxin ... is homogeneous by all
criteria tested including dodecyl sulphate gel electrophoresis under
non-reducing conditions, isoelelectric focussing and
immunodiffusion." (Tse 499; see Ans. 4, 5, 7 ("pure neurotoxin (mw
140 kda)")).
FF7. Tse teaches that "[w]hen this neurotoxin (5 mouse LD50 units; 60 pg
protein) was injected into rat hindleg muscle, it produced local
paralysis within 24 h." (Tse 498; see Ans. 3--4, 5, 7).
FF8. Tse teaches that "[a]s clearly demonstrated with impure neurotoxin
complexes ... , pure neurotoxin specifically and characteristically
inhibited stimulated and spontaneous release of acetylcholine at the
vertebrate neuromuscular junction" (Tse 499, col. 2 (internal citations
omitted)).
FF9. Simpson teaches "that botulinum toxin paralyzed what is now known
as the parasympathetic nervous system, but it did, not paralyze
postganglionic sympathetic transmission. Although not so stated,
their finding was that the toxin interrupted cholinergic transmission,
but it did not affect adrenergic transmission" (Simpson 166).
FFlO. Simpson teaches that "eight antigenically distinct toxin have been
identified (types, A, B. C1, C2, D, E, F and G) so strains are labeled
type A, type B, etc. According to the other scheme, the various strains
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Application 10/933,723
are divided into two groups, these being proteolytic and
nonproteolytic" (Simpson 156; Ans. 5 ("types A, B, C, D, E, F, and
G")). "[T]he molecular weights of the neurotoxins fall within the
range of 150,000 to 160,000" (Simpson 161, Ans. 5, 7, 8).
FF 11. Schantz, 8 cited by Appellants, discusses the properties of botulinum
toxins, including the purified neurotoxic component. According to
Schantz:
The nontoxic proteins bound to the neurotoxin apparently play
an important role in maintaining the toxic shape of the
neurotoxin. Careful handling of purified toxin is therefore
important for maintenance of stability. Botulinum toxin type A
is readily denatured by heat at temperatures above 40°C,
particularly at alkaline pH. Solutions of the toxin lose toxicity
when bubbles form at the air/liquid interface causing stretching
and pulling of the neurotoxin out of its toxic shape. This
denaturation also takes place in an atmosphere of nitrogen or
carbon dioxide. Dilution to extremely low concentrations
(nanograms per milliliter) also tends to decrease the stability of
the neurotoxin, but this can be prevented by diluting \~1ith a
buffered solution (at pH 6.8 or below) containing another
protein such as gelatin and certain albumins such as bovine or
human serum albumin. When the pH is raised above 7 .3, the
neurotoxin is liberated, which is very labile. Because of its
lability the neurotoxin is not practical for medical applications.
(Schantz 82, col. 2, internal citations omitted).
FF12. Schantz teaches:
Most recent information concerning the structure and
pharmacology of botulinum toxin has been obtained with
purified neurotoxins, but it is unlikely that these will be used in
a clinical setting. The toxin complexes are much more stable
8 Edward J. Schantz & Eric A. Johnson, Properties and Use of Botulinum
Toxin and Other Microbial Neurotoxins in Medicine, 56 MICROBIOL. REV.
80-99 ( 1992) (hereinafter "Schantz").
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Application 10/933,723
than neurotoxins and can be diluted and formulated with
retention of toxicity. Pure neurotoxins can be kept for several
weeks to months in solution in the cold but are inactivated on
dilution, formulation, and drying.
(Schantz 89, col. 2).
FF13. Schantz teaches:
we recommend that fresher batches of toxin periodically be
prepared to avoid detrimental changes that may occur on aging .
. . . Diluting a solution of botulinum toxin type A from a
concentration of 1 or 2 mg/ml to nanogram concentrations
causes detoxification unless another protein is added for
protection.
(Schantz 83, col. 2).
FF14.DasGupta9 teaches that the "pure NT is stable for months at pH 7.9
and 4 °C" and teaches that the neurotoxin:
isolated from the complex by ion-exchange chromatography,
first reported in 1966 ( 16) and now routinely prepared in
various laboratories (73, 48), has stable activity; Williams et al.
(81) have found that the homogenous preparation of type A NT,
stored at 4°C in 0.15 M TRIS/HCl buffer, pH 7.9, is stable for
several months. The pure preparations NT types A and E at
very low concentrations (such as 1x10-10 Mand lower) in
physiological buffers, with and without added gelatin or serum
albumin, are highly active (25, 48, 59, 73, 86) ....
REFERENCES
16. DasGupta BR, Boroff DA, Rothstein E. Chromatographic
fractionation of crystalline toxin of Clostridium botulinum type
A, Biochem Biophys Res Commun 1966;22:750-756.
9 Bibhuti R. DasGupta, Structures of Botulinum Neurotoxin, Its Functional
Domains, and Perspectives on the Crystalline Type A Toxin, in Therapy with
Botulinum Toxin 15-39 (J. Jankovic ed. 1994) (hereinafter "DasGupta").
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Application 10/933,723
48. Tse CK, Dolly JO, Hambleton P, Wray D, Melling J.
Preparation and characterization ofhomogenous neurotoxin
type A from Clostridium botulinum. Its inhibitory action on
neuronal release of acetylcholine in the absence and presence of
B-bungaro toxin. Eur J Biochem 1982; 122 :493-500.
59. Lomneth R, Suszkiw JB, DasGupta BR. Response of the
chick ciliary ganglion-iris neuromuscular preparation to
botulinum neurotoxin. Neurosci Lett 1990;113:211-216.
73. Sugii S, Sakaguchii G. Molecular construction of Clostridium
botulinum type A toxins. Infect Immun 1975; 12: 1262-1270.
81. Williams RS, Tse CK, Dolly JO, Hambleton P, Melling
J. Radio iodination of Botulinum Neurotoxin Type A with
Retention of Biological Activity and Its Binding to Brain
Synaptosomes. Eur. J. Biochem. 1983; 131 :437--445.
(DasGupta 31-32, 35-39).
FF15.Lamanna10 1988 discloses "a purified sample of type A toxin free of
hemagglutinin ... dissolved in a sterilized phosphate-0.2% gelatin
buffer (pH 6.2----6.7) for storage and i.v. injection" into mice, rats, and
dogs (Lamanna 1988, 70).
FF16.Lamanna 1988 teaches that "[h]emagglutinin-free toxin had the same
qualitative effects on the heart" as hemagglutinin-containing (i.e.,
complexed) toxin, but was more potent than the hemagglutinin-
containing toxin on a weight to weight basis (Lamanna 1988, 72).
FFl 7. The Specification's only disclosure regarding the neurotoxic
component is reproduced below:
The neurotoxic component of Botulinum toxin has a molecular
weight of about 150 kilodaltons and is thought to comprise a
1° C. Lamanna et al., Cardiac Effects of Botulinal Toxin, 293 ARCH. INT.
PHARMACODYN. THER. 69-83 (1988) (hereinafter "Lamanna 1988").
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short polypeptide chain of about 50 kD which is considered to
be responsible for the toxic properties of the toxin, i.e., by
interfering with the exocytosis of acetylcholine, by decreasing
the frequency of acetylcholine release, and a larger polypeptide
chain of about 100 kD which is believed to be necessary to
enable the toxin to bind to the presynaptic membrane.
(Spec. 2: 25 to 3: 2).
Principle of Law
[O]bviousness must be determined in light of all the facts, and
there is no rule that a single reference that teaches away will
mandate a finding of nonobviousness. Likewise, a given course
of action often has simultaneous advantages and disadvantages,
and this does not necessarily obviate motivation to combine.
See [Winner Int'! Royalty Corp. v. Wang, 202 F.3d 1340, 1349
n.8 (Fed. Cir. 2000)] ("The fact that the motivating benefit
comes at the expense of another benefit, however, should not
nullify its use as a basis to modify the disclosure of one
reference with the teachings of another. Instead, the benefits,
both lost and gained, should be weighed against one another.").
Where the prior art contains "apparently conflicting" teachings
(i.e., where some references teach the combination and others
teach away from it) each reference must be considered "for its
power to suggest solutions to an artisan of ordinary skill ....
consider[ing] the degree to which one reference might
accurately discredit another." In re Young, 927 F.2d 588, 591
(Fed. Cir. 1991).
Medichem, S.A. v. Rolabo, S.L.,437 F.3d 1157, 1165 (Fed. Cir. 2006).
Analysis
After considering the evidence and the arguments, we conclude the
weight of the evidence favors the Examiner's conclusion of obviousness.
Accordingly, we adopt the Examiner's reasoning (see Final Act. 3-8;
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Application 10/933,723
Grounds of Rejection, Ans. 4--9; FF I-FF IO), and agree that the Examiner
properly found Appellants' arguments unpersuasive (see Final Act. 8-25;
Response to Argument, Ans. 9-27). We address Appellants' arguments
below.
Appellants contend that "it is improper to ignore the fact that the
Schantz et al. reference also teaches away from the presently claimed
methods." (App. Br. 3) and that the Board "ignores the plain, express
language of the Schantz et al. reference" (App. Br. 12). Specifically,
Appellants argue that the following statements in Schantz teach away from
the claimed method:
Because of its lability the neurotoxin is not practical for medical
applications.
(App. Br. 12 (emphasis Appellants'); Schantz 82, col. 2).
Most recent information concerning the structure and
pharmacology ofbotulinum toxin has been obtained with
purified neurotoxins, but it is unlikely that these will be used in
clinical settings. The toxin complexes are much more stable
than neurotoxin and can be diluted and formulated with
retention of toxicity. Pure neurotoxins can be kept for several
weeks to months in solution in the cold but are inactivated on
dilution, formulation, and drying.
(App. Br. 12-13 (emphasis Appellants'); Schantz 89, col. 2).
In support of this argument, Appellants' submitted the Declaration of
Dr. Leonard A. Smith, whose work "has involved production, formulation,
and characterization of native botulinum toxin and recombinant neurotoxin
component fragments" (Deel. I, 11 i-f 9). Dr. Smith concludes that "a person
having ordinary skill in the art reading Schantz 1992 and considering the Tse
11 Declaration of Leonard A. Smith, PhD. (dated Nov. 20, 2007) (hereinafter
"Deel. I").
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et al. reference ... with or without consideration of the Lamanna [1988 and
1993] references clearly would have been discouraged from using the
neurotoxic component for human therapeutic purposes" based, at least in
part, on the statements quoted above (Deel. III 12, i-f 4).
There are, however, substantive and compelling inconsistencies
between Deel. I and Deel. III. Deel. I states that "[t]here is no doubt in my
mind and it is my opinion that the statements in Schantz 1992 that the
neurotoxic component is 'not practical for medical applications' and that the
neurotoxic component "'is unlikely .. (to) .. be used in a clinical setting"' are
clearly wrong" (Deel. I, i-f 15), while Deel. III states:
[ w ]hen considering all the facts presented in paragraph 15 of
my First Declaration with the exception of those from the
DasGupta reference and the Goodnough thesis, I conclude that
a person having ordinary skill in the art would not have
considered the statements within Schantz 1992 to be clearly
wrong.
(Deel. III, i-f 4; cf Deel. II, 13 i-f 4). Deel. III excludes the DasGupta reference
from the analysis, apparently because DasGupta itself is not prior art (see
Deel. III, i-f 3), but DasGupta was a review article that relied upon Williams,
a prior art reference, to evidence the stability of the purified neurotoxic
component (FF 14; cf Ans. 21) as well as a number of additional references
that teach neurotoxin isolation (FF 14 ).
Because the statements in Deel. II and III are inconsistent with Deel.
I, and Deel. II and III fail to consider the prior art teachings of Williams
12 Declaration of Leonard A. Smith, PhD. (dated Dec. 16, 2011) (hereinafter
"Deel. III").
13 Declaration of Leonard A. Smith, PhD. (dated May 25, 2011) (hereinafter
"Deel. II").
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relied upon by DasGupta, we find those statements' credibility reduced and
we afford them less weight. See Scripps Clinic & Res. Found. v. Genentech,
Inc., 927 F.2d 1565, 1578 (Fed. Cir. 1991) ("[A]pparent inconsistencies
among the three [expert] declarations raise questions of credibility and
weight").
We have, nonetheless, carefully considered Dr. Smith's Declarations.
However, we do not agree that Schantz teaches away from substituting the
neurotoxic component of botulinum toxin for the haemagglutinin-complexed
form of the toxin used by the Aoki patents. That is, we do not agree that
Schantz would have led one of ordinary skill in the art to expect that the
purified neurotoxin would be ineffective in treating excessive sweating as
there is ample evidence of record that the complexed toxin and the purified
neurotoxic component each produces the desired effect - local paralysis
(FF1-FF3, FF7)- and each operates by the same mechanism (FF8). While
we agree that one of ordinary skill in the art would have concluded from the
Schantz reference that the purified toxin is less practical in comparison with
the complexed toxin, Schantz also teaches that the purified neurotoxin can
be stored for weeks in the cold, and can be successfully diluted with careful
buffering and handling (FF11-FF13)-which is not unusual for therapeutic
agents.
Appellants contend that "the Board and the Examiner appear to
somehow base their various obviousness rejections for this family of
applications on the teachings of the Lamanna publications. As the record
indicates, the Lamanna references, however, are not cited in the current
obviousness rejections" (App. Br. 10), but Appellants also note that"[ w ]hen
assessing obviousness, the prior art as a whole including any evidence of
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teaching away must be considered. Medichem v. Rolabo, 437 F.3d 1157,
1166 (Fed. Cir. 2005)" (App. Br. 16 (emphasis Appellants')).
We agree with Appellants that the prior art must be assessed as a
whole in combination with the entirety of the evidence of record including
the Smith Declarations and the teachings of the Specification in order to
assess the overall power to suggest solutions to an artisan of ordinary skill.
We also agree with Appellants that no special weight is provided to
references relied upon by the Examiner (see App. Br. 16). 14
"When prior art contains apparently conflicting references, the Board
must weigh each reference for its power to suggest solutions to an artisan of
ordinary skill." In re Young, 927 F.2d 588, 591 (Fed. Cir. 1991). Moreover,
Although a reference that teaches away is a significant factor to
be considered in determining unobviousness, the nature of the
teaching is highly relevant, and must be weighed in substance.
A known or obvious composition does not become patentable
simply because it has been described as somewhat inferior to
some other product for the same use.
In re Gurley, 27 F.3d 551, 553 (Fed. Cir. 1994).
Lamanna 1988 is part of the record and prior art as a whole. Indeed,
the Examiner cites Appellants' own Reply Brief filed on February 24, 2009
in U.S. Application 10/461,829 that the "Lamanna and DasGupta
publication provide evidence that at the time the '996 parent application was
filed, purified neurotoxic component had been isolated, formulated, and
stored in stable form. Moreover, these publications provide evidence that
the neurotoxic component is sufficiently stable and active to be
14 With regard to Appellants' citation of an unrelated, nonprecedential PT AB
decision (see App. Br. 13-15), we note that "[e]ach case must be decided on
its own merits." In re Gyurik, 596 F.2d 1012, 1016 (CCPA 1979).
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administered intravenously" (Ans. 18; emphasis in original). Lamanna
1988, a prior art reference, supports this position, evidencing the storage and
use of the purified neurotoxin component for treatment of animals (FF 15).
Lamanna 1988 also found that the purified neurotoxin component was more
potent than the hemagglutinin-containing toxin on a weight to weight basis
(FF16). These teachings support the Examiner's position that the ordinary
artisan, weighing the teachings of the different references, would have had
reason to use the purified neurotoxin component as more potent, and would
have had a reasonable expectation of success in storing and using the
purified neurotoxin (FF 15 and FF 16).
When we consider the Schantz reference as a whole, together with the
Tse and Lamanna 1988 reference, we are not persuaded that one of ordinary
skill in the art would have been dissuaded from substituting the neurotoxic
component of botulinum toxin for the larger, more immunogenic
haemagglutinin-complexed form of the toxin in the prior art methods of
treating excessive sweating.
The Court of Customs and Patent Appeals has concluded that "[when
an] advantage is not disclosed in appellant's application" he is "not in a
favorable position to urge it as a basis for the allowance of claims." In re
Herr, 304 F.2d 906, 909 (1962) (internal citation and quotations omitted).
The Herr reasoning, though addressed to unexpected results and not
obviousness per se, is apt here, where the Specification has a single, limited
disclosure relating to the existence of a neurotoxic component ofbotulinum
toxin (FF 17) but provides no disclosure whatsoever on methods of purifying
the neurotoxic component, methods of stably storing a purified neurotoxic
component, or any clinical method for using the purified neurotoxic
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component. In sum, the Specification provides no guidance on how to make
or use "a therapeutically effective amount of a single or di chain form of the
neurotoxic component" as required by claim 115, fully relying upon the prior
art to enable and disclose this teaching.
Thus, to the extent that Appellants rely upon the purified neurotoxic
component as a distinguishing limitation, their own Specification is solely
enabled for patient administration of a purified neurotoxic component by the
prior art, not by any teachings disclosed by Appellants.
Appellants contend that "DasGupta specifically corroborates
Appellant[s'] position that Schantz would have discouraged one of ordinary
skill from clinical use of the neurotoxic component" citing DasGupta's
teaching that "this prevailing view needs rectification" (Reply Br. 3, citing
DasGupta 31 (emphasis Appellants')). Appellants contend:
[i]f a person having ordinary skill in the art as of December
1993 already knew that Dr. Schantz's statements were incorrect
as the Examiner repeatedly insists is the case, then the
statements within the DasGupta reference are nonsensical as
there would have been no prevailing view needing rectification
as of 1994.
(Reply Br. 3).
15 We note, but do not rely upon, the absence of any requirement in claim 1
for purification of the neurotoxic component. This would have provided the
Examiner a reasonable basis to interpret claim 1 broadly to encompass
botulinum toxin including both the neurotoxic component and
haemagglutinin component, consistent with the Specification's reliance
solely on commercially available botulinum toxin that includes both
components and the absence of any disclosure in the Specification teaching
purifying the neurotoxic component. Under this claim interpretation, which
we do not rely upon, the primary references would have anticipated claim 1
(see Spec. 3: 5-14).
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Application 10/933,723
We do not find this argument persuasive because DasGupta is not
relying upon newly disclosed post filing date evidence from 1994, but rather
expressly relies upon prior art references to establish the functionality of the
purified neurotoxin, specifically stating:
Williams et al. (81) have found that the homogeneous
preparation of type A NT, stored at 4°C in 0.15 M TRIS-HCl
buffer, pH 7.9, is stable for several months. The pure
preparations of NT types A and E at very low (such as 1 x 10-
10 Mand lower) in physiological buffers, with and without
added gelatin or serum albumin, are highly active
(25 ,48,59 '73 ,86).
(DasGupta 32). As already noted, Williams was published in 1983 (FF14).
The other references cited by DasGupta were published from 1966 to 1990
(FF 14; cf Ans. 21) and reasonably establish that DasGupta was relying on
knowledge in prior art regarding storage and use of the purified neurotoxin,
not post-filing date information.
CONCLUSION OF LAW
The Examiner has established that treating a spastic muscle by
administering the neurotoxic component of a botulinum toxin, rather than a
complexed form of the botulinum toxin, would have been obvious over the
evidence of record.
SUMMARY
We affirm the rejection of claim 1 under the judicially created
doctrine of nonstatutory obviousness-type double patenting over Aoki '886
in view of Tse and Simpson. Claims 21, 22, and 31-39 were not separately
argued and fall with claim 1. 37 C.F.R. § 41.37 (c) (1) (iv).
We affirm the rejection of claim 1 under the judicially created
doctrine of nonstatutory obviousness-type double patenting over Aoki '049
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Appeal2013-006105
Application 10/933,723
in view of Tse and Simpson. Claims 21, 22, and 31-39 were not separately
argued and fall with claim 1.
We affirm the rejection of claim 1 under the judicially created
doctrine of nonstatutory obviousness-type double patenting over Aoki '578
in view of Tse and Simpson. Claims 21, 22, and 31-39 were not separately
argued and fall with claim 1.
TIME PERIOD FOR RESPONSE
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a).
AFFIRMED
19