Ex Parte Carpenter et alDownload PDFBoard of Patent Appeals and InterferencesJul 24, 201210271832 (B.P.A.I. Jul. 24, 2012) Copy Citation UNITED STATES PATENT AND TRADEMARKOFFICE 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. 10/271,832 10/16/2002 John F. Carpenter 42830-00247 9883 13586 7590 07/24/2012 Endo Pharmaceuticals Inc. c/o Marsh Fischmann & Breyfogle LLP 8055 East Tufts Avenue, Suite 450 Denver, CO 80237 EXAMINER GUPTA, ANISH ART UNIT PAPER NUMBER 1654 MAIL DATE DELIVERY MODE 07/24/2012 PAPER 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. PTOL-90A (Rev. 04/07) UNITED STATES PATENT AND TRADEMARK OFFICE __________ BEFORE THE BOARD OF PATENT APPEALS AND INTERFERENCES __________ Ex parte JOHN F. CARPENTER, JEFFREY B. ETTER, and ADRIAN C. SAMANIEGO __________ Appeal 2011-010470 Application 10/271,832 Technology Center 1600 __________ Before DEMETRA J. MILLS, ERIC GRIMES, and MELANIE L. McCOLLUM, Administrative Patent Judges. GRIMES, Administrative Patent Judge. DECISION ON APPEAL This is an appeal under 35 U.S.C. § 134 involving claims to a pharmaceutical product. The Examiner has rejected the claims as anticipated and lacking adequate description in the Specification. We have jurisdiction under 35 U.S.C. § 6(b). We reverse. STATEMENT OF THE CASE The Specification discloses that “stable concentrated protein formulations can be prepared without requiring lyophilization. The Appeal 2011-010470 Application 10/271,832 2 concentrated protein formulation is a mixture of the protein in precipitated form and a liquid medium, typically an aqueous medium.” (Spec. 2: 27-30.) The concentrated formulations are prepared by “precipitation of a protein of interest from a solution . . . with a suitable precipitating agent; followed by removal of sufficient liquid from the resulting mixture to prepare a concentrated mixture comprising . . . preferably at least 10 weight percent of the precipitated protein” (id. at 3: 12-16). Suitable precipitating agents include polyoxyalkylene block copolymers (id. at 9: 15-16). Claims 2-24, 54, 56-61, and 82-107 are on appeal. Claim 23 is representative and reads as follows: 23. A pharmaceutical product, comprising a pharmaceutical composition contained within a sealed container, wherein: the pharmaceutical composition comprises: (i) polyoxyalkylene block copolymer; (ii) at least 10 weight percent, relative to weight of the pharmaceutical composition, of a precipitated protein, the precipitated protein being in the form of a precipitate having been prepared by precipitation from an aqueous liquid solution with the polyoxyalkylene block copolymer; and (iii) at least 10 weight percent, relative to the weight of the pharmaceutical composition, water. The claims stand rejected as follows: • Claims 2-23, 54, 56-61, and 82-107 under 35 U.S.C. § 112, first paragraph, for lack of adequate written description (Answer 3) and • Claims 2, 4-11, 13, 14, 16-24, 54, 56-61, 83-85, 87-95, and 97-105 under 35 U.S.C. § 102(b) as anticipated by Kwak1 (Answer 7). 1 Kwak et al., U.S. Patent 5,861,158, Jan. 19, 1999. Appeal 2011-010470 Application 10/271,832 3 I. The Examiner has rejected all of the claims on appeal except claim 24 for lack of adequate written description, on the basis that the Specification does not describe the structural characteristics that allow a protein to be precipitated with a polymer precipitating agent (Answer 5). The Examiner cites Stratton2 as evidence that “[n]ot all peptides of greater than 15 Kda form[ ] a precipitate in an aqueous liquid solution with the biocompatible polymer precipitating agent and the precipitate is at least 10% by weight” (id.). The Examiner also finds that “the claims are open to any polymer material” but the Specification does not describe “what structural attributes the polymer must contain to effectively precipitate the protein” (id. at 6). Appellants argue that the claims are not directed to new chemical substances, but to “a mixture including known ingredients, with one ingredient being a protein-polyoxyalkylene block copolymer precipitate, and with the mixture being highly concentrated in that precipitate ingredient” (Appeal Br. 8). Appellants argue that one of skill in the art would recognize that they were in possession of the full scope of the claimed invention based on the Specification’s description (id. at 10-15). With regard to the Examiner’s finding that the Specification does not adequately describe the polymer in the claimed composition, Appellants argue that “all of the claims rejected for lack of written description specifically require that the polymer is a polyoxyalkylene block copolymer” (id. at 16). 2 Stratton et al., Drug Delivery Matrix Containing Native Protein Precipitates Suspended in a Poloxamer Gel, 86 J. PHARM. SCI. 1006-1010 (1997). Appeal 2011-010470 Application 10/271,832 4 “[T]he examiner bears the initial burden, on review of the prior art or on any other ground, of presenting a prima facie case of unpatentability.” In re Oetiker, 977 F.2d 1443, 1445 (Fed. Cir. 1992). With respect to the written description requirement of 35 U.S.C. § 112, first paragraph, “the test for sufficiency is whether the disclosure of the application relied upon reasonably conveys to those skilled in the art that the inventor had possession of the claimed subject matter as of the filing date.” Ariad Pharms., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1351 (Fed. Cir. 2010) (en banc). We agree with Appellants that the Examiner has not carried the burden of showing that a person of ordinary skill in the art would not have considered the Specification’s description to show that Appellants were in possession of the claimed invention. The Specification describes a “method of preparing pharmaceutical compositions including a protein” (Spec. 3: 8- 9): [T]he method involves precipitation of a protein of interest from a solution in which the protein is dissolved by contacting the solution with a suitable precipitating agent; followed by removal of sufficient liquid from the resulting mixture to prepare a concentrated mixture comprising at least 8 weight percent of the precipitated protein, and preferably at least 10 weight percent of the precipitated protein. (Id. at 3: 12-16.) See also id. at 13, ll. 3-13 (“During the liquid separation [step], sufficient liquid is removed to provide the desired concentration of the precipitated protein in the concentrated mixture.”). The Specification states that “[i]t is not . . . necessary that the protein be highly concentrated in the solution” prior to precipitation (id. at 6: 10). “Rather, it is generally preferred that the concentration of the protein in the Appeal 2011-010470 Application 10/271,832 5 solution is relatively low, for ease of preparation and handling of the solution during processing” (id. at 6: 11-12). The Specification states that the “protein used with the method of the present invention can be any protein for which a highly concentrated formula is desired” (id. at 6: 17-18). Thus, the Specification describes a composition resulting from a process in which a protein in solution is mixed with a precipitating agent such as a polyoxyalkylene block copolymer, and then liquid is removed from the precipitated protein/polymer mixture until the desired protein concentration is reached. The Specification states that the process can be practiced with any desired protein, and does not state that the protein must have any particular structural characteristics to make it appropriate for inclusion in the claimed composition. The Examiner cites no persuasive evidence to show that structure of a protein affects its ability to be concentrated to at least 10% by weight as a polymer/protein precipitate. The Examiner finds that “Stratton et al. teaches a formulation of chymotrypsin with poloxamer 407 which did not produce a precipitate of at least 10% by weight[]” (Answer 5). However, the Examiner has not pointed to any specific disclosure in Stratton that shows a failed attempt to make a composition comprising containing at least 10% protein in a protein/polymer precipitate. Stratton describes making a protein suspension of α-chymotrypsin and poloxamer 407 in which the final protein concentration was 20mg/mL (Stratton 1006-1007). The Examiner has not, however, pointed to any disclosure in Stratton of a liquid separation step such as that described in the Specification as necessary to concentrate the protein/polymer precipitate to a desired concentration. Thus, Stratton does Appeal 2011-010470 Application 10/271,832 6 not provide evidence that casts doubt on the Specification’s statement that the claimed compositions can be made with any desired protein, regardless of its structural characteristics. With regard to the Examiner’s finding that the claims also lack adequate description because they “are open to any polymer material” (Answer 6), we agree with Appellants that all of the claims rejected on this basis are limited to a polyoxyalkylene block copolymer. The Examiner has not provided any persuasive basis for finding that a skilled worker would not recognize, based on the Specification’s description, that Appellants are in possession of a composition comprising a polyoxyalkylene block copolymer. In summary, the Examiner has not provided an adequate basis for finding that the claims on appeal lack adequate written description in the Specification. We therefore reverse the rejection of claims 2-23, 54, 56-61, and 82-107 under 35 U.S.C. § 112, first paragraph. II. The Examiner has rejected claims 2, 4-11, 13, 14, 16-24, 54, 56-61, 83-85, 87-95, and 97-105 as anticipated by Kwak (Answer 7). The Examiner finds that Kwak discloses “a polymeric formulation compris[ing] 2.5% pluronic L121, tween 80 and phosphate buffered saline (see col. 6, lines 56-65) is mixed with myeloma IgG (see col. 7)” (id. at 7-8). The Examiner acknowledges that Kwak does not describe the mixture as forming a precipitate, but finds that “such a result would be inherent in light of the claims” (id. at 8). The Examiner also finds that the protein content recited in the claims would be inherent in Kwak’s mixture, reasoning as follows: Appeal 2011-010470 Application 10/271,832 7 The claims do not recite a specific concentration of the polymer nor a specific concentration for the peptide. The claims only state that the protein precipitates when mixed with the a [sic] biocompatible polymer precipitating agent. IgG has a molecular weight of greater than 15kD. Thus, when the protein is mixed with pluronic L121, a precipitate of at least 10%-99% would inherently be achieved. (Id.) Appellants argue that, among other deficiencies, the composition in Kwak that the Examiner finds to be anticipatory contains a protein concentration that is much lower than the 10% by weight that is required by the claims (Appeal Br. 29-33). We agree with Appellants that the Examiner has not made a prima facie case that Kwak identically disclose the claimed invention. The Examiner relies on Kwak’s disclosure of a composition comprising, among other things, 2.5% pluronic L121 and myeloma IgG (Answer 7-8, citing Kwak at cols. 6-7). Pluronic L121 is described in the Specification as a polyoxyalkylene block copolymer that is suitable for use as a precipitating agent (Spec. 9: 30 to 10: 13). Kwak therefore describes a composition containing a protein and a polyoxyalkylene block copolymer. However, the claims require a composition comprising at least 10 weight percent of precipitated protein (see, e.g., claim 23). The Examiner points to the composition described in Kwak at columns 6 to 7. That composition contains one milliliter of an adjuvant containing Tween-80, Pluronic L121, and squalane in phosphate buffered saline (see Kwak, col. 6, l. 57 to col. 7, l. 3) and one milliliter of a solution of myeloma idiotype protein conjugated to keyhole limpet hemocyanin (“Id- KLH”) (id. at col. 7, ll. 3-6). One milliliter of the Id-KLH solution “yielded Appeal 2011-010470 Application 10/271,832 8 a patient dose of 0.5 mg of Id” (id. at col. 6, ll. 54-55). Thus, the composition cited by the Examiner as anticipatory contained approximately 1 mg of Id-KLH conjugate (assuming that the conjugate contains equal parts Id and KLH) in a volume of 2 mL, or a protein concentration of about 0.5 mg/mL. As Appellants have argued, the protein concentration in Kwak’s composition is far below what is required by the claims, since 10% by weight would correspond to approximately 100 mg/mL in Kwak’s water- based composition (since one milliliter of water weighs one gram, or 1000 mg). The Examiner has pointed to no disclosure of a liquid separation step in Kwak, like the step described in the instant Specification as necessary to concentrate a protein/polymer precipitate to a desired concentration. Thus, the Examiner has not made a prima facie showing that Kwak expressly or inherently discloses a composition that meets all of the limitations of the claims on appeal. The rejection of claims 2, 4-11, 13, 14, 16-24, 54, 56-61, 83-85, 87-95, and 97-105 as anticipated by Kwak is therefore reversed. SUMMARY We reverse the rejection of claims 2-23, 54, 56-61, and 82-107 for lack of adequate written description and the rejection of claims 2, 4-11, 13, 14, 16-24, 54, 56-61, 83-85, 87-95, and 97-105 as anticipated by Kwak. REVERSED lp Copy with citationCopy as parenthetical citation