Application of Fisher

• Decision Date: 11 June 1970
• Docket Number: Patent Appeal No. 8208.
• Citation: 427 F.2d 833
• Parties: Application of Joseph D. FISHER.
• Court: U.S. Court of Customs and Patent Appeals (CCPA)

427 F.2d 833 (1970)

Application of Joseph D. FISHER.

Patent Appeal No. 8208.

United States Court of Customs and Patent Appeals.

June 11, 1970.

Carl C. Batz, Frank T. Barber, Chicago, Ill., attorneys of record, for appellant. George R. Jones, Robert H. Berdo, Beale & Jones, Arlington, Va., of counsel.

Joseph Schimmel, Washington, D. C., for the Commissioner of Patents. Jack E. Armore, Washington, D. C., of counsel.

Before RICH, Acting Chief Judge, ALMOND, BALDWIN, and LANE, Judges, and MATTHEWS, Senior Judge, United States District Court for the District of Columbia, sitting by designation.

LANE, Judge.

This appeal is from the decision of the Patent Office Board of Appeals, which affirmed the rejection of claims 4 and 5, the only claims remaining in appellant's application serial No. 72,481, filed November 29, 1960, for Adrenal Gland Stimulating Concentrate and Method for the Preparation Thereof. The application is a continuation-in-part of a prior co-pending application serial No. 435,451, filed June 9, 1954, which was before this court in In re Fisher, 307 F.2d 948, 50 CCPA 1025 (1962). That application was a continuation of application serial No. 122,588, filed October 20, 1949, which we shall refer to as the parent application.

THE DISCLOSURE

The instant specification relates to the preparation of substances containing adrenocorticotrophic hormones (ACTH) in a composition suitable for injection into human beings in the treatment of certain forms of arthritis and other human pathological conditions. It is stated that previous ACTH products were unsatisfactory for administration to humans because of their low potency, generally around 50% of "International Standard," and because of their relatively high content of undesirable factors, notably posterior pituitary hormones which consist mainly of oxytocic and vasopressor principles. A method¹ is disclosed for producing ACTH preparations having potencies ranging from 111% to 230% of standard and containing no more than 0.08 units of vasopressin and no more than 0.05 units of oxytocin per International Unit of ACTH, which limits are said to be tolerable to humans. The method generally starts with frozen pituitary glands of hogs, sheep, beef or other animals, including whales. These glands are quick-thawed in an organic solvent to extract contaminated ACTH from the gland meat. A precipitate containing the active material is recovered, free of contaminants, by treatment with fractionating salts. The material is then subjected to hydrolysis, and an inactive fraction of hydrolized fragmented material is separated from a fraction containing the active substance. The active fraction is then adjusted to a pH above 2.8, the excess salts being separated from the concentrate of the active principle. Several variations of this procedure are set forth and six specific examples are given. The specification then states that the ACTH concentrate produced as described is found to contain peptides having free amino and carboxyl groups, and is further characterized

by its solubility in glacial acetic acid and phenol; by its relative insolubility in other organic solvents; by its greater stability under acid conditions than under alkali conditions; by its susceptibility to attack by proteolytic enzymes and peptidases; and by its positive reaction to the Millon and xanthoproteic tests for tyrosine, the biuret test for peptide linkage, the ninhydrin test for free amino groups in the alpha position, the Sakaguchi test for guanidine groups, and the Hopkins-Gole and benzaldehyde tests for indole nuclei and tryptophane.

The specification then states that the product can be characterized structurally as a peptide containing a chain of identifiable amino acids. While the exact sequence will vary from product to product, depending on the source and preparative history of the product, the first 24 amino acids in the chain, counting from the N terminus of the molecule, will have the following sequence: (1) Serine, (2) Tyrosine, (3) Serine, (4) Methionine, (5) Glutamic Acid, (6) Histadine, (7) Phenylalanine, (8) Arginine, (9) Tryptophan, (10) Glycine, (11) Lysine, (12) Proline, (13) Valine, (14) Glycine, (15) Lysine, (16) Lysine, (17) Arginine, (18) Arginine, (19) Proline, (20) Valine, (21) Lysine, (22) Valine, (23) Tyrosine, (24) Proline. ACTH obtained from hogs contains a sequence of 39 amino acids, the first 24 being as recited above; AC TH obtained from sheep or beef also contains a sequence of 39 amino acids, the first 24 being as recited, and the 25th to 39th being in a sequence different from that of the hog extract.² No structural description is given for ACTH extracted from other animals.

THE CLAIMS

Appellant defines the subject matter sought to be patented as follows:

4. An adrenocorticotrophic hormone preparation containing at least 1 International Unit of ACTH per milligram and containing no more than 0.08 units of vasopressin and no more than 0.05 units of oxytocin per International Unit of ACTH, and being further characterized as containing as the active component of a? polypeptide of at least 24 amino acids having the following sequence from the N terminus of the molecule; Serine, Tyrosine, Serine, Methionine, Glutamic Acid, Histadine, Phenylalanine, Arginine, Tryptophan, Glycine, Lysine, Proline, Valine, Glycine, Lysine, Lysine, Arginine, Arginine, Proline, Valine, Lysine, Valine, Tyrosine, Proline.

5. An adrenocorticotrophic hormone preparation containing at least 1 International Unit of ACTH per milligram and containing no more than 0.08 units of vasopressin and no more than 0.05 units of oxytocin per International Unit of ACTH, and being further characterized by its solubility in glacial acetic acid and phenol; by its relative insolubility in other organic solvents; by its greater stability under acid conditions than under alkali conditions; by its susceptibility to attack by proteolitic enzymes and peptidases; and by its positive reaction to the Millon and xanthoproteic tests for tyrosine, the biuret test for peptide linkages, and the ninhydrin test for free amino groups in the alpha position, the Sakaguchi test for guanidine groups, and the Hopkins-Gole and benzaldehyde tests for indole nuclei and tryptophane.

OPINION

There are many grounds of rejection affirmed by the board in this case. We shall set them forth separately, with our opinion on each.

(a) The res judicata rejection

The board affirmed the examiner's rejection of claim 5 on the ground of res judicata, stating that the claim differed from claim 13 in Fisher, supra, "mainly in calling for a `preparation containing at least 1 International Unit of ACTH per milligram' in place of the terminology in claim 13 `concentrate having a potency at least equal to that of the International Standard.'" The board held this to be "no significant difference other than in verbiage." We reverse the board on this ground of rejection. "Verbiage" was the very problem in Fisher. The court there found that the words "a potency at least equal to the International Standard" rendered the claims unpatentable under the second paragraph of 35 U.S.C. § 112. 307 F.2d at 950-951, 50 CCPA at 1029. These words do not appear in the claims before us. Thus, a different issue is presented and res judicata does not apply. See In re Fried, 312 F.2d 930, 50 CCPA 954 (1963).

(b) The rejection on the Li references

The examiner rejected claim 4 under 35 U.S.C. § 102 as anticipated by the following references:

Li et al. (III), Science, vol. 124, p. 934 (Nov. 9, 1956).

Li et al., J.A.C.S., vol. 80, No. 10, pp. 2587-88 (May 20, 1958).

Appellant did not contest the pertinence of these references, but sought to remove them by relying on his parent application which, as mentioned above, was filed in 1949. The examiner took the position that appellant was not entitled to the parent date under 35 U.S.C. § 120 because the parent contained insufficient disclosure to support claim 4 in the manner required by the first paragraph of 35 U.S.C. § 112. The board affirmed this rejection for two reasons. First, since the parent application lacked any structural description of the ACTH extracts therein disclosed, the Board concluded that it could not be determined whether those products would meet the terms of claim 4, which recites a specific sequence of the first 24 amino acids. Appellant contended that the parent application inherently disclosed products meeting the terms of claim 4, even though appellant did not know the chemical structure of those products when the parent application was filed. Appellant cited several cases in support of the proposition that inherent disclosure is sufficient under 35 U.S.C. § 112, including Riester v. Kendall, 159 F.2d 732, 34 CC PA 859 (1947), and In re Nathan, 328 F.2d 1005, 51 CCPA 1059 (1964). The board did not dispute the correctness of this proposition, but found that "it has not been established that the parent disclosures inherently produce the claimed products * * *." We agree with appellant that this finding was erroneous. The parent application discloses treatment of hog pituitary extracts. The Li (J.A.C.S.) article discloses the amino acid sequence for beef ACTH and states that the first 24 amino acids in the sequence are the same for porcine (hog) ACTH, namely, the sequence recited in claim 4. The hog-extracted products disclosed in appellant's parent application must therefore have had the recited sequence. The board's second reason for holding the parent application insufficient to support claim 4 was that the products disclosed in the parent were insufficient to support a claim of the breadth of claim 4. On this point we agree with the board. The claim recites that the product must contain "at least" 24 amino acids in a specified sequence. The parent disclosure mentions treating extracts from "hog, beef, lamb, and other animal pituitary glands, and including also pituitary glands of whales."...