Alton, In re

• Decision Date: 05 February 1996
• Docket Number: No. 94-1495,94-1495
• Citation: 76 F.3d 1168,37 USPQ2d 1578
• Parties: In re Norman K. ALTON, Mary A. Peters, Yitzhak Tabinsky, and David L. Snitman.
• Court: U.S. Court of Appeals — Federal Circuit

Page 1168

76 F.3d 1168

37 U.S.P.Q.2d 1578

In re Norman K. ALTON, Mary A. Peters, Yitzhak Tabinsky, and

David L. Snitman.

No. 94-1495.

United States Court of Appeals,

Federal Circuit.

Feb. 5, 1996.

Michael F. Borun, Marshall, O'Toole, Gerstein, Murray & Borun, Chicago, Illinois, argued for appellants. With him on the brief was Li-Hsien Rin-Laures. Also on the brief was Steven M. Odre, Thousand Oaks, California. Of counsel were Robert R. Cook and Ron K. Levy, Thousand Oaks, California.

Scott A. Chambers, Associate Solicitor, Office of the Solicitor, Arlington, Virginia, argued for appellee. With him on the brief were Nancy J. Linck, Solicitor, Albin F. Drost, Deputy Solicitor and Richard Torczon, Associate Solicitor.

Before MICHEL, Circuit Judge, FRIEDMAN, Senior Circuit Judge, and SCHALL, Circuit Judge.

SCHALL, Circuit Judge.

Appellants Norman K. Alton, et al. ("Alton"), appeal the ruling of the United States Patent and Trademark Office Board of Patent Appeals and Interferences ("Board") in Appeal No. 94-3098. In its decision, the Board held that the specification of application serial number 06/483,451 ("the '451 application") did not provide adequate written descriptive support for the amino acid sequence of human gamma interferon ("IFN-K") described in claim 70. We vacate the decision and remand the case to the Board for further proceedings.

BACKGROUND

I.

IFN-K is a protein secreted by cells in the human immune system to stimulate immunological activity. ¹ Patrick W. Gray et al., Expression of Human Immune Interferon cDNA in E. Coli and Monkey Cells, 295 Nature 503 (1982). IFN-K is believed useful because it activates macrophages, which are a class of cells in the immune system. Bruce Alberts et al., Molecular Biology of the Cell 1048, 1049 (2d ed. 1989). IFN-K is composed of a sequence of 146 amino acids. ² The complete sequence is divided into four subunits. IFN-K polypeptides containing alterations in the naturally-occurring amino acid sequence are called "analogs."

Claim 70 of the '451 application, set forth below, recites an analog of IFN-K:

[Met ^-1, des-Cys ¹, des-tyr ², des-cys ³] IFN-K polypeptide produced by a DNA sequence coding therefor in a transformant organism, said product having substantially the characteristics of human immune interferon.

(brackets in original). The bracketed words at the beginning of the claim indicate how the claimed IFN-K differs from the natural version of IFN-K. ³ "Met," "cys," and "tyr" are abbreviations for three of the twenty amino acids; they stand for methionine, cysteine, and tyrosine, respectively. A positive superscripted number following the abbreviation of an amino acid indicates the position of that amino acid in the 146 amino acid chain that comprises IFN-K. For example, "tyr ²" means that tyrosine is the second amino acid in the 146 amino acid chain. The designation "des" preceding the name of the amino acid indicates that that particular amino acid has been deleted and no amino acid has been substituted in its place. Therefore, "[des-cys ¹, des-tyr ², des-cys ³]" means that the cysteine at position one of the amino acid chain In sum, the analog of IFN-K recited in claim 70 has two characteristics that distinguish it from the natural version of IFN-K. First, as "[des-cys ¹, des-tyr ², des-cys ³]" indicates, the first three amino acids--cysteine, tyrosine, and cysteine--of the natural 146 amino acid sequence have been deleted from the claimed IFN-K analog. These three amino acids are located on the fourth subunit ("IF-4") of the complete sequence. Second, methionine has been placed at the beginning of the amino acid sequence of the claimed analog.

                has been removed, as has the tyrosine at position two and the cysteine at position three.   A negative superscripted number indicates that an amino acid has been added onto the beginning (the N-terminus) of the IFN-K sequence.   Thus, "met -1" means that a methionine has been placed at the beginning of the IFN-K amino acid chain
                

The '451 application's specification contains twelve examples of IFN-K analogs. Of these, Example 5 is closest to the analog that is the subject of claim 70. Like claim 70, it discloses deletion of the first three amino acids and placement of methionine at the beginning of the amino acid sequence of IFN-K ("[met ^-1, des-cys ¹, des-tyr ², des-cys ³]"). Unlike claim 70, however, Example 5 additionally discloses substitution of asparagine--the eighty-first amino acid in the IFN-K chain--with lysine, another amino acid ("lys ⁸¹"). The eighty-first amino acid is located on the second subunit ("IF-2") of the IFN-K sequence.

II.

The '451 application was filed April 15, 1983. It is a continuation-in-part of a parent application filed on May 6, 1982, and later abandoned. The examiner issued a final rejection of the claims of the '451 application as anticipated under 35 U.S.C. § 102(e) and rendered obvious over the prior art under 35 U.S.C. § 103.

Alton appealed the examiner's final rejection to the Board. On February 28, 1991, the Board reversed the examiner's section 102 and 103 rejections but rejected the claims on the new ground that the specification failed to describe adequately the subject matter of the claims, as required by 35 U.S.C. § 112, p 1. The Board stated: "The closest analog to that claimed herein is described [in Example 5]. This particular analog, though similar to that claimed herein, does not constitute a description of the claimed analog."

Electing further prosecution pursuant to 37 C.F.R. 1.196(b), ⁴ Alton submitted to the examiner, in response to the Board's section 112, p 1 rejection, a declaration by Dr. Randolph Wall (the "Wall declaration"). In due course, the examiner issued a final rejection on the same grounds as had the Board. Alton then requested reconsideration; the examiner denied the request and maintained his rejection ("final rejection").

Alton appealed the final rejection of claim 70 to the Board. The examiner filed his Answer and the Board sustained the section 112, p 1 rejection on June 21, 1994. In its decision, the Board held that "the specific polypeptide of claim 70 was not described in the original specification of application Serial No. 06/483,451." The Board adopted the examiner's dismissal of the Wall declaration, in which the examiner reasoned that the declaration was opinion evidence rather than factual evidence. The examiner stated, "Little weight is given an opinion affidavit on the ultimate legal question at issue." This appeal followed.

DISCUSSION

I.

The issue of whether a patent specification adequately describes the subject

                matter claimed is a question of fact.  Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1563, 19 USPQ2d 1111, 1116 (Fed.Cir.1991).   We review questions of fact arising from Board rejections under a clearly erroneous standard.  In re Caveney, 761 F.2d 671, 674, 226 USPQ 1, 3 (Fed.Cir.1985).   We review questions of law de novo.  Electronic Design & Sales, Inc. v. Electronic Data Systems Corp., 954 F.2d 713, 715, 21 USPQ2d 1388, 1390 (Fed.Cir.1992)
                

II.

Alton contends that the Board committed clear error in holding that the '451 specification did not describe the subject matter of claim 70. Alton additionally argues that the Board erred in failing to give substantial weight to the Wall declaration.

The adequate written description requirement of 35 U.S.C. § 112, p 1, provides that

[t]he specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.

(emphasis added).

The adequate written description requirement, which is distinct from the enablement and best mode requirements, ⁵ serves "to ensure that the inventor had possession, as of the filing date of the application relied on, of the specific subject matter later claimed by him; how the specification accomplishes this is not material." In re Wertheim, 541 F.2d 257, 262, 191 USPQ 90, 96 (CCPA 1976). In order to meet the adequate written description requirement, the applicant does not have to utilize any particular form of disclosure to describe the subject matter claimed, but "the description must clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed." In re Gosteli, 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed.Cir.1989) (citation omitted). Put another way, "the applicant must ... convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention." Vas-Cath, 935 F.2d at 1563-64, 19 USPQ2d at 1117. Finally, we have stated that "[p]recisely how close the original description must come to comply with the description requirement of section 112 must be determined on a case-by-case basis." Eiselstein v. Frank, 52 F.3d 1035, 1039, 34 USPQ2d 1467, 1470 (Fed.Cir.1995) (quoting Vas-Cath, 935 F.2d at 1561, 19 USPQ2d at 1116).

As noted above, following the Board's decision of February 28, 1991, Alton elected further prosecution pursuant to 37 C.F.R. § 1.196(b). In that context, Alton submitted the Wall declaration in response to the Board's section 112, p 1 rejection. In paragraph 9J of his declaration, Dr. Wall addressed the issue of whether Example 5 in the specification described what was claimed in claim 70: ⁶

J. The specific modifications of subunit IF-4 for deleting both cysteines and the intermediate tyrosine at amino acid positions 1, 2, and 3 are set out at page 50, lines 11 and 12, which describe modification of the IF-4 subunit (which contains a methionyl residue-specifying codon at position -1) to contain the codons,

5'-ATG CAG-3'

3'-TAC GTC-5'

in the amino acid specifying region. ATG is a...