Ex Parte Anderson et al

Patent Trial and Appeal Board

Dec 16, 2016

13072109 (P.T.A.B. Dec. 16, 2016)

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.
13/072,109 03/25/2011 DAVID M. ANDERSON 204257-0011-01US-496374 5308
55694 7590 12/20/2016
DRINKER BIDDLE & REATH (DC)
1500 K STREET, N.W.
SUITE 1100
WASHINGTON, DC 20005-1209
EXAMINER
PAGUIO FRISING, MICHELLE F
ART UNIT PAPER NUMBER
1651
NOTIFICATION DATE DELIVERY MODE
12/20/2016 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):
DB RIPDocket @ dbr. com
penelope. mongelluzzo @ dbr. com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte DAVID M. ANDERSON, HUMG-YU HSIAO, and LIN LIU
Appeal 2015-008093
Application 13/072,109
Technology Center 1600
Before DONALD E. ADAMS, JOHN G. NEW, and DAVID COTTA,
Administrative Patent Judges.
ADAMS, Administrative Patent Judge.
DECISION ON APPEAL1
This appeal under 35 U.S.C. § 134(a) involves claims 31—34 and
48—57 (App. Br. 2).2 Examiner entered rejections under 35 U.S.C. § 101
and 35 U.S.C. § 103(a). We have jurisdiction under 35 U.S.C. § 6(b).
We AFFIRM.
1 Appellants identify the real party in interest as “ELI LILLY AND
COMPANY” (App. Br. 2).
2 Pending “[cjlaims 37-46 [stand] withdrawn from consideration” (App. Br.
2)
Appeal 2015-008093
Application 13/072,109
STATEMENT OF THE CASE
Appellants disclose “compositions and methods for reducing
immunological stress and improving animal growth performance” (Spec.
12). Appellants’ claims 31 and 54 are representative and reproduced below:
31. An oral composition comprising an immune stress-
reducing enzyme in an orally acceptable carrier, wherein said
composition is selected from the group consisting of:
(i) an animal feed comprising at least 20 IU of said
immune stress-reducing enzyme/kg feed;
(ii) a liquid composition other than an animal feed
comprising at least 2,000,000 IU of said immune stress-
reducing enzyme/L; and
(iii) a solid composition other than an animal feed
comprising at least 40,000 IU of said immune stress-reducing
enzyme/kg,
wherein said immune stress reducing enzyme is a
bacterial alkaline phosphatase.
(App. Br. 29.)
54. The composition of claim 34, wherein the alkaline
phosphatase is present in an amount of at least 200,000 IU per
kilogram of the solid composition.
(App. Br. 32.)
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The claims stand rejected as follows:
Claims 31—33 and 48—53 stand rejected under 35 U.S.C. § 103(a) as
unpatentable over the combination of Kiss,3 Merck,4 Short,5 Rosenberg,6
and Possemiers.7
Claims 31—34 and 48—56 stand rejected under 35 U.S.C. § 103(a) as
unpatentable over the combination of Kiss, Merck, Short, Rosenberg,
Possemiers, and Brands.8
Claims 31—34 and 48—57 stand rejected under 35 U.S.C. § 103(a) as
unpatentable over the combination of Kiss, Merck, Short, Rosenberg,
Possemiers, Brands, and Rippie.9
Claims 31, 32, 34, and 54—56 stand rejected under 35 U.S.C. § 103(a)
as unpatentable over the combination of Brands and Short.
Claims 31, 32, 34, and 54—57 stand rejected under 35 U.S.C. § 103(a)
as unpatentable over the combination of Brands, Short, and Rippie.
3 Kiss, WO 2004/054609 Al, published July 1, 2004.
4 Merck KGaA Calbiochem® Catalogue, Product No. 524545 Phosphatase,
Alkaline, E. coli (2014). We recognize that Examiner’s Final Action
incorrectly relies on Merck KGaA Calbiochem® Catalogue, Product No.
524604 Phosphatase, Alkaline, Human Placenta (2014) disclosing human
alkaline phosphatase (see Final Act. 11). Examiner’s Answer corrects the
error in the Final Action and directs attention to Merck’s description of the
E. coli Alkaline Phosphatase (see Ans. 21—22).
5 Short et al., US 2002/0164751 Al, published Nov. 7, 2002.
6 Rosenberg, US 2006/0099200 Al, published May 11, 2006.
7 Possemiers et al., US 2009/0130724 Al, published May 21, 2009.
8 Brands, WO 2005/074978 Al, published Aug. 18, 2005.
9 Edward G. Rippie, Ph.D., Remington’s Pharmaceutical Sciences, Ch. 89:
1585—1602 (17th ed., Gennaro, et al., ed., Mack Publishing Co., Easton, PA)
(1985).
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Application 13/072,109
Claims 31—34 and 48—57 stand rejected under 35U.S.C. § 101, as
directed to non-statutory subject matter.
Obviousness:
ISSUE
Does the preponderance of evidence relied upon by Examiner support
a conclusion of obviousness?
FACTUAL FINDINGS (FF)
FF 1. Examiner finds that “Kiss discloses a preparation comprising human
alkaline phosphatase or a derivative thereof in a physiologically acceptable
carrier,” such as “physiological saline, liposomes, or other [known] delivery
systems,” and “a method of using [the preparation] for reducing blood
glucose level in a mammal,” wherein “[t]he alkaline phosphatase [] can be
obtained from commercial sources like Sigma and Calbiochem, or through
extraction of placental tissue, chemical synthesis, or recombinant methods”
(Final Act. 8, citing Kiss 9: 24—31, 10: 1—11, and 17: 1—11; see also Final
Act. 9 (Examiner finds “alkaline phosphatase in saline [] suitable for feeding
to an animal”)).
FF 2. Examiner finds that Kiss discloses a preparation comprising “about
1-30 mg of alkaline phosphatase per milliliter of preparation” (Final Act.
10).
FF 3. Examiner finds that Kiss fails to disclose “bacterial alkaline
phosphatase” and relies on Short to disclose that E. coli is “one of the two
dominant commercial sources of alkaline phosphatase” (Final Act. 9; see
Short 112).
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Application 13/072,109
FF 4. Examiner relies on Rosenberg and Possemiers to disclose the
administration of bacterial enzymes, other than alkaline phosphatase, to
humans (Final Act. 9—10).
FF 5. Examiner relies on Merck to disclose the activity of bacterial
alkaline phosphatase (Ans. 21—22; see also Merck (disclosing the activity of
E. coli alkaline phosphatase as “>500 units/ml”).
FF 6. Brands discloses
compositions comprising a source of [alkaline phosphatase
(AP) that] are suitable for oral administration^ which] comprise
an enteric coating to protect the AP from the adverse effects of
gastric juices and low pH. . . . Enteric coating compositions[,
which are known] in the art may comprise [] a solution of a
water-soluble enteric coating polymer mixed with the active
ingredient(s) such as AP and other excipients, which are
dispersed in an aqueous solution and which may subsequently
be dried and/or pelleted.
(Brands 15: 4—11; see Final Act. 16.)
FF 7. Examiner finds that “Rippie teaches that a [solid composition can be
modified such that it takes the form of a powder] through various established
techniques such as crushing, grinding, and milling” (Final Act. 18; see also
id. at 24—25).
FF 8. Brands discloses
compositions comprising a source of AP ... are particularly
suited for oral administration to prevent[,] reduce, treat or
alleviate inflammatory diseases of the gastrointestinal tract.
Inflammatory diseases of the gastrointestinal tract may be
induced and/or exacerbated significantly by the influx of
[lipopolysaccharides (LPS)]. A reduction in the amount of
toxic LPS in the lumen of the intestines by administration of
sources of AP will, through detoxification of the lipid A moiety
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Application 13/072,109
of LPS, result in a corresponding decrease in the systemic
influx of toxic LPS in the circulation of a subject.
(Brands 12: 23—32; see Final Act. 20.)
FF 9. Brands exemplifies the administration of an “a single oral dose of
75,000 U/kg [bovine intestinal alkaline phosphatase (BIAP), to mice,] per
oral gavage (in 250 pi autoclaved drinking water)” (Brands 24: 8—9; Final
Act. 20).
FF 10. Brands discloses that “AP containing compositions for the delivery
of AP at mucosal tissues for detoxification of LPS according to [Brands’]
invention preferably comprise an eukaryotic AP” (Brands 15: 15—17
(emphasis added); see also id. at 10: 2-4 (Brands discloses that “native or
recombinant micro-organisms, such as bacteria, fungi, protozoa and yeast
may be applied as a source of AP in the context of [Brands’] invention”)).
FF 11. Examiner finds that Brands fails to disclose bacterial alkaline
phosphatase and relies on Short to disclose that “A. coli is one of the two
dominant commercial sources of alkaline phosphatase” (Final Act. 21; see
Short 112).
ANALYSIS
The rejection over the combination of Kiss, Merck, Short, Rosenberg,
Possemiers, with or without Brands alone or in combination with Rippie:
Based on the combination of Kiss, Merck, Short, Rosenberg,
Possemiers, Examiner concludes that, at the time Appellants’ invention was
made, it would have been prima facie obvious to “have replaced Kiss[’s]
human placental alkaline phosphatase with Short[’]s bacterial alkaline
phosphatase,” because Rosenberg and Possemiers establish that “bacterial
enzymes are generally regarded as safe [for administration] to humans”
(Final Act 10; see FF 1 4). Examiner reasons that the combination of Kiss,
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Short, Rosenberg, and Possemiers reads on Appellants’ claimed
concentration of bacterial alkaline phosphatase, in view of Merck (see Ans.
21-22 ; see FF 5). In this regard, Examiner asserts that Merck discloses that
E. coli alkaline phosphatase has “a specific activity of about 500 units/mg,”
which, when read in light of Kiss’ disclosure of a composition comprising
1—30 mg/ml of human placental phosphatase, “translates to [a] composition
having a concentration of about 500,000-15,000,000 IU/L alkaline
phosphatase” (Ans. 21—22). We are not persuaded.
As Appellants explain, Examiner misinterpreted Merck’s disclosure
(Reply Br. 6—7). In this regard, Appellants correctly contend that,
notwithstanding Examiner’s assertion to the contrary, Merck discloses an
activity of “500 U/ml, not 500 U/mg” (id. at 6; see FF 5). Thus, as
Appellants’ explain, Examiner’s conclusion is based on a mathematical error
(Reply Br. 6—7; see id. at n. 6 (Appellants correctly contend that,
notwithstanding Examiner’s mathematical error, following Examiner’s
reasoning would lead to a concentration of E. coli phosphatase, which has a
lower limit of 500 mg*U/ml2)).
Brands and Rippie, as relied upon by Examiner in combination with
Kiss, Merck, Short, and Rosenberg, to respectively disclose solid
compositions comprising alkaline phosphatase and that a powder can be
obtained by crushing, grinding, or milling a solid composition, fail to make
up for the foregoing deficiency in Examiner’s combination of Kiss, Merck,
Short, and Rosenberg (see Final Act. 15—19; FF 6—7).
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The rejection over the combination of Brands and Short'.
Based on the combination of Brands and Short, Examiner concludes
that, at the time Appellants’ invention was made, it would have been prima
facie obvious to use bacterial alkaline phosphatase, as suggested Short, as
the source of alkaline phosphatase in Brands’ composition (see Final Act.
21; FF 8—11). In this regard, we note that while Brands prefers the use of an
alkaline phosphatase from an eukaryotic source (FF 10), we find that a
reference disclosure is not limited only to its preferred embodiments, but is
available for all that it discloses and suggests to one of ordinary skill in the
art. See In reLamberti, 545 F.2d 747, 750 (CCPA 1976).
Claim 54:
Examiner finds that the combination of Brands and Short fails to
disclose a solid composition comprising the amount of alkaline phosphatase
required by Appellants’ claim 54 (Final Act. 22). Examiner reasons,
however, that a person of ordinary skill in this art would have found it prima
facie obvious to modify Brands’ disclosure of the administration of alkaline
phosphatase to mice at a concentration of 75,000 IU/kg to include a larger
“concentration when said composition is intended to be for treatment of a
bigger mammal such as a human” (id.). See In re Geisler, 116 F.3d 1465,
1470 (Fed. Cir. 1997), quoting In reAller, 220 F.2d 454, 456 (CCPA 1955),
(“it is not inventive to discover the optimum or workable ranges by routine
experimentation.”).
Appellants contend that Brands’ disclosure of an alkaline
phosphatase concentration of “‘75,000 IU/kg’ ... at best relates to a liquid
dose of. . . bovine alkaline phosphatase per oral gavage (in 250 pi
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Application 13/072,109
autoclaved drinking watery (App. Br. 25, footnote omitted). To the extent
that Appellants’ contend that a person of ordinary skill in this art would not
have found it prima facie obvious, based on the combination of Brands and
Short, to: (1) administer alkaline phosphatase as a solid or a liquid and/or
(2) utilize bacterial alkaline phosphatase, we are not persuaded (see id.).
The combination of Brands and Short disclose the administration of
alkaline phosphatase as a liquid or a solid (see FF 6 and 9). In addition,
Brands discloses that alkaline phosphatase, within the scope of Brands’
disclosure, may be obtained from a bacterial source (see FF 10). We are not
persuaded by Appellants’ contention that the “kg” unit, in Brands’
concentration of 75,000 U/kg, relates to “the body weight of the mouse, not
to a solid composition comprising alkaline phosphatase” and, therefore,
Brands fails to disclose a solid composition comprising at least 200,000 IU
of alkaline phosphatase/kg of the solid composition (App. Br. 25, n. 9).
Appellants’ fail to provide persuasive evidence or argument to support
a conclusion that, notwithstanding Examiner’s conclusion to the contrary,
the combination of Brands and Short fails to make obvious a solid
composition comprising bacterial alkaline phosphatase, wherein the bacterial
alkaline phosphatase is present in the solid composition at a concentration of
at least 40,000 IU/kg as required by Appellants’ claim 31 (see Final Act. 22—
23; Ans. 29-30; see also FF 6 and 8—11). In this regard, we are not
persuaded by Appellants’ intimation that a person of ordinary skill in this art
would not have found it prima facie obvious to optimize the concentration of
bacterial alkaline phosphatase to the particular animal being treated and, in
that regard, optimize, through routine experimentation, the components of a
solid composition comprising bacterial alkaline phosphatase for the
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particular application it is used for, including the relative amount of enzyme
per total kg weight of the solid composition. See In re Geisler, 116 F.3d at
1470.
Claim 31\
Examiner concludes that the combination of Brands and Short
discloses a “solid composition containing] 75,000 IU/Kg of [bacterial]
alkaline phosphatase . . . and fulfills the limitation [in Appellants’ claim 31]
that the composition is ‘a solid composition other than an animal feed
comprising at least 40,000 IU of [bacterial alkaline phosphatase]
enzyme/kg (Final Act. 20).
For the reasons set forth above, we are not persuaded by Appellants’
contentions that a person of ordinary skill in this art would not “have had a
reason to change the amount and administration form of alkaline
phosphatase in Brands” (App. Br. 25). In addition, the combination of
Brands and Short suggest a solid composition comprising bacterial alkaline
phosphatase for use in preventing, reducing, treating, or alleviating
“inflammatory diseases of the gastrointestinal tract,” which “may be induced
and/or exacerbated significantly by the influx of [lipopolysaccharides
(LPS)]” (FF 8).
Therefore, we are not persuaded by Appellants’ contention that a
person of ordinary skill in this art would not have found it prima facie
obvious to utilize the composition, made obvious by the combination of
Brands and Short, “for the reduction of immune stress in an animal” (App.
Br. 25—26). In this regard, we find that Appellants have, at best, discovered
a new benefit derived from the use of a composition, made obvious by the
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combination of Brands and Short, which cannot render patentable Brands’
composition for use in preventing, reducing, treating, or alleviating
inflammatory disease of the gastrointestinal tract. See generally In re Huai-
Hung Kao, 639 F.3d 1057, 1071 (Fed. Cir. 2011); In re Woodruff, 919 F.2d
1575, 1578 (Fed. Cir. 1990).
For the foregoing reasons, we are not persuaded by Appellants’
contention that “[t]he claimed bacteria, oral administration route and AP
concentrations were not recognized to be result effective variables for the
reduction of immune stress at the time of filing” and, thus, “[a]ny
optimization to treat LPS-mediated or—exacerbated diseases is irrelevant to
the present” composition claimed by Appellants (App. Br. 26). For the
foregoing reasons, we are not persuaded by Appellants’ contentions
regarding their alleged surprising and unexpected results regarding the use
of a composition, made obvious by the combination of Brands and Short, for
“reduc[ing] immune stress when administered to animals as evidenced by
the [Anderson] Declaration submitted August 27, 2014” (id.; cf Ans. 29-
30).
Brands discloses the use of alkaline phosphatase from bacterial
sources, such as those disclosed by Short (FF 10-11). Therefore, we are not
persuaded by Appellants’ contention that a person of ordinary skill in this art
would not have found it prima facie obvious to utilize bacterial alkaline
phosphatase in Brands’ composition (App. Br. 26).
The rejection over the combination of Brands, Short, and Rippie:
Based on the combination of Brands, Short, and Rippie, Examiner
concludes that, at the time Appellants’ invention was made, it would have
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been prima facie obvious to covert the solid composition suggested by the
combination of Brands and Short to a powder by following Rippie’s
methodology of producing a powder from a solid (Final Act. 24—25).
Having found no deficiency in the combination of Brands and Short,
we are not persuaded by Appellants’ contention “that Rippie does not
remedy the deficiencies in Brands and Short” (App. Br. 27).
CONCLUSION OF LAW
The preponderance of evidence relied upon by Examiner fails to
support a conclusion of obviousness with respect to the rejections over the
combination of Kiss, Merck, Short, Rosenberg, Possemiers, with or without
Brands alone or in combination with Rippie.
The rejection of claims 31—33 and 48—53 under 35 U.S.C. § 103(a) as
unpatentable over the combination of Kiss, Merck, Short, Rosenberg, and
Possemiers is reversed.
The rejection of claims 31—34 and 48—56 under 35 U.S.C. § 103(a) as
unpatentable over the combination of Kiss, Merck, Short, Rosenberg,
Possemiers, and Brands is reversed.
The rejection of claims 31—34 and 48—57 under 35 U.S.C. § 103(a) as
unpatentable over the combination of Kiss, Merck, Short, Rosenberg,
Possemiers, Brands, and Rippie is reversed.
The preponderance of evidence relied upon by Examiner supports a
conclusion of obviousness with respect to the combination of Brands and
Short with or without Rippie.
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Application 13/072,109
The rejection of claims 31 and 54 under 35 U.S.C. § 103(a) as
unpatentable over the combination of Brands and Short is affirmed. Claims
32, 34, 55, and 56 are not separately argued and fall with claim 31.
The rejection of claim 31 under 35 U.S.C. § 103(a) as unpatentable
over the combination of Brands, Short, and Rippie is affirmed. Claims 32,
34, and 54—57 are not separately argued and fall with claim 31.
Utility.
ISSUE
Does the evidence of record support Examiner’s finding that
Appellants’ claimed invention is directed to non-statutory subject matter?
ANALYSIS
We adopt as our own the findings and reasons set forth by Examiner
(Ans. 17—20). Moreover, we agree with Examiner that the composition set
forth in Appellants’ claim 31 represents patent-ineligible subject matter;
specifically, a composition comprising the combination of two naturally
occurring products: (1) ‘“bacterial alkaline phosphatase’” and (2) “‘an
orally acceptable carrier,’ [which] encompasses natural products like water,
saline, grass, and grains” (see Ans. 19). In this regard, we find no error in
Examiner’s conclusion that the bacterial alkaline phosphatase concentrations
set forth in Appellants’ claim 31 are “not sufficient to render the claim[]
significantly different from what is found in nature because the recited
concentrations do not [result in a] structural change [in either naturally
occurring product] and do not produce new characteristics or new function”
(Ans. 20). Stated differently, the elements of Appellants’ claimed invention
when considered individually or “as an ordered combination” do not
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“transform the nature of the claim” into patent-eligible subject matter. See
Alice Corp. Pty. Ltd. v. CLS Bank Inti, 134 S. Ct. 2347, 2355 (2014),
quoting Mayo Collaborative Servs. v. Prometheus Labs., Inc., 132 S. Ct.
1289, 1297 (2012).
On this record, Appellants’ failed to establish an evidentiary basis to
support a conclusion that placing bacterial alkaline phosphatase in, for
example, water changes the structure, function, or other properties of the
bacterial alkaline phosphatase or water. In addition, Appellants failed to
establish an evidentiary basis to support a conclusion that the amount of
bacterial alkaline phosphatase in, for example, water results in markedly
different characteristics of the bacterial alkaline phosphatase or the claimed
composition as a whole. Further, as discussed above, the combination of
bacterial alkaline phosphatase and an orally acceptable carrier to formulate a
composition was “well-understood, routine, conventional activity already
engaged in by the scientific community” and “when viewed as a whole, add
nothing significant beyond the sum of their parts taken separately” (see
generally FF 6 and 8—11). See, e.g., Mayo, 132 S. Ct. at 1298; see also Funk
Brothers Seed Co. v. Kalo Inoculant Co., 333 U.S. 127, 131 (1948).
For the foregoing reasons, we are not persuaded by Appellants’
contention that “the recited concentrations, let alone [] the recited
combination^],” set forth in the composition of Appellants’ claim 31, do not
exist in nature or that the intended use of the composition, somehow,
transforms the claimed composition into patent-eligible subject matter
(Reply Br. 4—5). For the same reasons, we are not persuaded by Appellants’
contention that the amount of bacterial alkaline phosphatase in an orally
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acceptable carrier “does not cut off or significantly impede other uses of the
individual components that comprise the [composition]” (Reply Br. 5—6).
CONCLUSION OF LAW
The evidence of record supports Examiner’s finding that Appellants’
claimed invention is directed to non-statutory subject matter. The rejection
of claim 31 under 35 U.S.C. § 101, as directed to non-statutory subject
matter. Claims 32—34 and 48—57 are not separately argued and fall with
claim 31.
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
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