Amgen Inc. v. F. Hoffmann-LaRoche LTD et al

Filing 502

DECLARATION re #498 MOTION for Summary Judgment of No Obviousness-Type Double Patenting BY HARVEY F. LODISH, Ph.D. by Amgen Inc.. (Attachments: #1 Exhibit A#2 Exhibit B#3 Exhibit C#4 Exhibit D-1#5 Errata D-2#6 Exhibit D-3#7 Errata D-4#8 Exhibit E-1#9 Exhibit E-2 (part 1)#10 Exhibit E-2 (part 2)#11 Exhibit E-3#12 Exhibit E-4#13 Exhibit E-5 (part 1)#14 Exhibit E-5 (Part 2)#15 Exhibit E-5 (part 3)#16 Exhibit E-6)(Gottfried, Michael)

Amgen Inc. v. F. Hoffmann-LaRoche LTD et al

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Exhibit C

Lodish Decl re Amgen's Motion for SJ of No ODP
Dockets.Justia.com

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EXHIBIT C Claims and Groups Relating to Restriction Requirement Restriction Group Group I: Polypeptide Claim Language 1. A purified and isolated polypeptide having part or all of the primary structural conformation and one or more of the biological properties of naturally-occurring erythropoietin and characterized by being the product of prokaryotic or eukaryotic expression of an exogenous DNA sequence. 2. A polypeptide according to claim 1 further characterized by being free of association with any mammalian protein. 3. A polypeptide according to claim 1 wherein the exogenous DNA sequence is a cDNA sequence. 4. A polypeptide according to claim 1 wherein the exogenous DNA sequence is a manufactured DNA sequence. 5. A polypeptide according to claim 1 wherein the exogenous DNA sequence is a genomic DNA sequence. 6. A polypeptide according to claim 1 wherein the exogenous DNA sequence is carried on an autonomous replicating circular DNA plasmid or viral vector. 7. A polypeptide according to claim 1 possessing part or all of the primary structural conformation of human erythropoietin as set forth in Table VI or any naturally occurring allelic variant thereof. 8. A polypeptide according to claim 1 possessing part or all of the primary structural conformation of monkey erythropoietin as set forth in Table V or any naturally occurring allelic variant thereof. 9. A polypeptide according to claim 1 which has the immunological properties of naturally-occurring erythropoietin. 10. A polypeptide according to claim 1 which has the in vivo biological activity of naturally-occurring erythropoietin. 11. A polypeptide according to claim 1 which has the in vitro biological activity of naturally-occurring erythropoietin. 12. A polypeptide according to claim 1 further characterized by

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Restriction Group

Claim Language being covalently associated with a detectable label substance. 13. A polypeptide according to claim 12 wherein said detectable label is a radiolabel. 16. A polypeptide product of the expression of a DNA sequence of claim 14 in a prokaryotic or eukaryotic host. 39. A polypeptide product of the expression in a prokaryotic or eukaryotic host cell of a DNA sequence according to claims 17 or 34. 40. A glycoprotein product having a primary structural conformation sufficiently duplicative of that of a naturally-occurring erythropoietin to allow possession of one or more of the biological properties thereof and having an average carbohydrate composition which differs from that of naturally-occurring erythropoietin. 41. A glycoprotein product having a primary structural conformation sufficiently duplicative of that of a naturally-occurring human erythropoietin to allow possession of one or more of the biological properties thereof and having an average carbohydrate composition which differs from that of naturally-occurring human erythropoietin. 47. A synthetic polypeptide having part of all of the amino acid sequence as set forth in Table V and having one or more of the in vivo or in vitro biological activities of naturally-occurring monkey erythropoietin. 48. A synthetic polypeptide having part of all of the amino acid sequence as set forth in Table VI, other than a sequence of residues entirely within the sequence numbered 1 through 20, and having a biological property of naturally-occurring human erythropoietin. 49. A synthetic polypeptide having part of all of the secondary conformation of part or all of the amino acid sequence set forth in Table VI, other than a sequence of residues entirely within the sequence numbered 1 through 20, having a biological property of naturallyoccurring human erythropoietin. 50. A process for the production of a polypeptide having part of all of the primary structural conformation and one or more of the biological properties of naturally-occurring erythropoietin, said process comprising: growing, under suitable nutrient conditions, prokaryotic or eukaryotic host cells transformed or transfected with a DNA vector according to claim 37, and isolating desired polypeptide products of the expression of DNA sequences in said vector.

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Restriction Group

Claim Language 51. An antibody substance characterized by immunoreactivity with erythropoietin and with a synthetic polypeptide having a primary structural conformation substantially duplicative of a continuous sequence of amino acid residues extant in naturally-occurring erythropoietin except for any polypeptide comprising a sequence of amino acid residues entirely comprehended within sequence, A-P-P-R-L-I-C-D-S-R-V-L-E-R-Y-L-LE-A-K. 52. An antibody according to claim 51, which is a monoclonal antibody. 53. An antibody according to claim 51, which is a polyclonal antibody. 54. An antibody according to claim 51, which is immunoreactive with erythropoietin and a synthetic polypeptide having eh sequence selected from the sequences: V-P-D-T-K-V-N-F-Y-A-W-K-R-M-E-V-G; K-E-A-I-S-P-P-D-A-A-S-A-A; V-Y-S-N-F-L-R-G-K-L-K-L-Y-T-G-E-AC-R-T-G-D-R. 59. A polypeptide product of the expression of a DNA sequence according to claim 58 in a prokaryotic or eukaryotic host cell.

Group II: DNA

14. A DNA sequence for use in securing expression in a prokaryotic or eukaryotic host cell of a polypeptide product having at least a part of the primary structural conformation and one or more of the biological properties of naturally-occurring erythropoietin, said DNA sequence selected from among: (a) the DNA sequence set out in Tables V and VI or their complementary strands; (b) DNA sequences which hybridize to the DNA sequences defined in (a) or fragments thereof; and (c) DNA sequences which, but for the degeneracy of the genetic code, would hybridize to the DNA sequences defined in (a) or (b). 15. A prokaryotic or eukaryotic host cell transformed or transfected with a DNA sequence according to claim 14 in a manner allowing the host cell to express said polypeptide product. 17. A purified and isolated DNA sequence coding for prokaryotic or eukaryotic host expression of a polypeptide having part or all of the primary structural conformation and one or more of the biological activities of erythropoietin.

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Restriction Group

Claim Language 18. A cDNA sequence according to claim 17. 19. A monkey species erythropoietin coding DNA sequence according to claim 18. 20. A DNA sequence according to claim 19 and including the protein coding region set forth in Figure 5. 21. A genomic DNA sequence according to claim 17. 22. A human species erythropoietin coding DNA sequence according to claim 21. 23. A DNA sequence according to claim 22 and including the protein coding region set forth in Figure 6. 24. A manufactured DNA sequence according to claim 17. 25. A manufactured DNA sequence according to claim 24 and including one or more codons preferred for expression in E. coli cells. 26. A manufactured DNA sequence according to claim 25, coding for expression of human species erythropoietin. 27. A manufactured DNA sequence according to claim 26 including the protein coding region set forth in Figure 7. 28. A manufactured DNA sequence according to claim 24 and including one or more codons preferred for expression in yeast cells. 29. A manufactured DNA sequence according to claim 28, coding for expression of human species erythropoietin. 30. A manufactured DNA sequence according to claim 29 including the protein coding region set forth in Figure 8. 31. A DNA sequence according to claim 17 covalently associated with a detectable label substance. 32. A DNA sequence according to claim 31 wherein the detectable label is a radiolabel. 33. A single-strand DNA sequence according to claim 31. 34. A purified and isolated DNA sequence coding for a

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Restriction Group

Claim Language polypeptide fragment or polypeptide analog of naturally-occurring erythropoietin. 35. A DNA sequence coding for [Phe15]hEPO, [Phe49]hEPO, [Phe ]hEPO, [His7]hEPO, [Asn2 des- Pro2 through Ile6]hEPO, [des-Thr163 through Arg166]hEPO, or [27-55]hEPO.
145

36. A DNA sequence according to claim 34 which is a manufactured sequence. 58. A purified and isolated DNA sequence as set out in Figure 5 or 6 or a fragment thereof or the complementary strand of such a sequence or fragment. 61. A biologically functional circular plasmid or viral DNA vector including a DNA sequence according to claim 14. 62. A prokaryotic or eukaryotic host cell stably transformed or transfected with a DNA vector according to claim 61. 63. A biologically functional circular plasmid or viral DNA vector including a DNA sequence according to claim 17. 64. A prokaryotic or eukaryotic host cell stably transformed or transfected with a DNA vector according to claim 63. 65. A biologically functional circular plasmid or viral DNA vector including a DNA sequence according to claim 34. 66. A prokaryotic or eukaryotic host cell stably transformed or transfected with a DNA vector according to claim 65. 67. A biologically functional circular plasmid or viral DNA vector including a DNA sequence according to claim 35. 68. A prokaryotic or eukaryotic host cell stably transformed or transfected with a DNA vector according to claim 67. 69. A process for the production of a polypeptide having part or all of the primary structural conformation and one or more of the biological activities of naturally-occurring erythropoietin, said process comprising: growing, under suitable nutrient conditions, prokaryotic or eukaryotic host cells transformed or transfected with a DNA vector according to claim 62, and isolating desired polypeptide products of the expression of DNA sequences in said vector.

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Restriction Group

Claim Language 70. A process for the production of a polypeptide having part or all of the primary structural conformation and one or more of the biological activities of naturally-occurring erythropoietin, said process comprising: growing, under suitable nutrient conditions, prokaryotic or eukaryotic host cells transformed or transfected with a DNA vector according to claim 63, and isolating desired polypeptide products of the expression of DNA sequences in said vector. 71. A process for the production of a polypeptide having part or all of the primary structural conformation and one or more of the biological activities of naturally-occurring erythropoietin, said process comprising: growing, under suitable nutrient conditions, prokaryotic or eukaryotic host cells transformed or transfected with a DNA vector according to claim 65, and isolating desired polypeptide products of the expression of DNA sequences in said vector. 72. A process for the production of a polypeptide having part or all of the primary structural conformation and one or more of the biological activities of naturally-occurring erythropoietin, said process comprising: growing, under suitable nutrient conditions, prokaryotic or eukaryotic host cells transformed or transfected with a DNA vector according to claim 67, and isolating desired polypeptide products of the expression of DNA sequences in said vector.

Group III: Plasmid

37. A biologically functional circular plasmid or viral DNA vector including a DNA sequence according to either of claims 14, 17, 34 or 35. 38. A prokaryotic or eukaryotic host cell stably transformed or transfected with a DNA vector according to claim 37.

Group IV: Cells

42. Vertebrate cells which can be propagated in vitro continuously and which upon growth in culture are capable of producing in the medium of their growth in excess of 100 U of erythropoietin per 106 cells in 48 hours as determined by radioimmunoassay. 43. Vertebrate cells according to claim 42 capable of producing in excess of 500 U erythropoietin per 106 cells in 48 hours. 44. Vertebrate cells according to claim 42 capable of producing in excess of 1,000 U erythropoietin per 106 cells in 48 hours. 45. Vertebrate cells according to claim 42 which are mammalian

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Restriction Group or avian cells.

Claim Language

46. Vertebrate cells according to claim 45 which are COS-1 cells or CHO cells. Group V: Pharmaceutical Composition 55. A pharmaceutical composition comprising an effective amount of a polypeptide according to claims 1, 16, 39, 40 or 41 and a pharmaceutically acceptable diluent, adjuvant or carrier. 56. A method for providing erythropoietin therapy to a mammal comprising administering an effective amount of a polypeptide according to claims 1,16, 39, 40 or 41. 57. A method according to claim 56 wherein the therapy comprises enhancing hematocrit levels. Group VI: Assay 60. An improvement in the method for detection of a specific single stranded polynucleotide of unknown sequence in a heterogeneous cellular or viral sample including multiple single-stranded polynucleotides wherein: (a) a mixture of labeled single-stranded polynucleotide probes is prepared having uniformly varying sequences of bases, each of said probes being potentially specifically complementary to a sequence of bases which is putatively unique to the polynucleotide to be detected; (b) the sample is fixed to a solid substrate; (c) the substrate having the sample fixed thereto is treated to diminish further binding of polynucleotides thereto except by way of hybridization to polynucleotides in said sample; (d) the treated substrate having the sample fixed thereto is transitorily contacted with said mixture of labeled probes under conditions facilitative of hybridization only between totally complementary polynucleotides; and (e) the specific polynucleotide is detected by monitoring for the presence of a hybridization reaction between it and a totally complementary probe within said mixture of labeled probes, as evidenced by the presence of a higher density of labeled material on the substrate at the locus of the specific polynucleotide in comparison to a background density of labeled material resulting from non-specific binding of labeled probes to the substrate, said improvement comprising using in excess of 32 mixed probes and

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Restriction Group

Claim Language performance of one or more of the following: (1) employing a nylon-based paper as said solid substrate; (2) treating with a protease in step (c); (3) employing individual labeled probe concentrations of approximately 0.025 picomoles; and (4) employing as one of the hybridization conditions in step (d) stringent temperatures approaching to with 4°C away from the lowest calculated Td of any of the probes employed.

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