DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Status of Application, Amendments and/or Claims
The amendment, filed 19 September 2022, has been entered in full. The amendment, filed 10 March 2023, has been entered in full. Claims 3-10 are amended. New claims 18-27 are added. Claims 1-10, 18-27 are under examination.
Foreign Priority
Acknowledgment is made of applicant’s claim for foreign priority under 35 U.S.C. 119 (a)-(d). The certified copy EPO 20164619.7 (filed 3/20/2020) has been placed of record in the file.
Information Disclosure Statement
The information disclosure statement(s) (IDS) (filed 9/19/2022 and 3/10/2023) were received and comply with the provisions of 37 CFR §§1.97, 1.98 and MPEP § 609. They have been placed in the application file and the information referred to therein has been considered as to the merits.
Nucleotide and/or Amino Acid Sequence Disclosures
Summary of Requirements for Patent Applications Filed On Or After July 1, 2022, That Have Sequence Disclosures
37 CFR 1.831(a) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.831(b) must contain a “Sequence Listing XML”, as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.831-1.835. This “Sequence Listing XML” part of the disclosure may be submitted:
1. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter “Legal Framework”) in XML format, together with an incorporation by reference statement of the material in the XML file in a separate paragraph of the specification (an incorporation by reference paragraph) as required by 37 CFR 1.835(a)(2) or 1.835(b)(2) identifying:
a. the name of the XML file
b. the date of creation; and
c. the size of the XML file in bytes; or
2. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation by reference statement of the material in the XML format according to 37 CFR 1.52(e)(8) and 37 CFR 1.835(a)(2) or 1.835(b)(2) in a separate paragraph of the specification identifying:
a. the name of the XML file;
b. the date of creation; and
c. the size of the XML file in bytes.
SPECIFIC DEFICIENCIES AND THE REQUIRED RESPONSE TO THIS NOTICE ARE AS FOLLOWS:
Specific deficiency - Sequences appearing in the specification are not identified by sequence identifiers (i.e., “SEQ ID NO:X” or the like) in accordance with 37 CFR 1.831(c).
The specification lists a sequence that does not have an accompanying SEQ ID NO. Please see page 30, line 1.
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required sequence identifiers, consisting of:
• A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
• A copy of the amended specification without markings (clean version); and
• A statement that the substitute specification contains no new matter.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The 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 or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The 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.
Claims 7, 22, 23 and 27 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The specification has written description for:
“…wherein the first VEGF molecule has 100% amino acid sequence identity to SEQ ID NO:3 and wherein the second VEGF molecule has 100% amino acid sequence identity to SEQ ID NO: 4…”
But lacks written description for
“…wherein the first VEGF molecule has at least 50% (or at least 90%) amino acid sequence identity to SEQ ID NO:3 and wherein the second VEGF molecule has at least 50% (or at least 90%) amino acid sequence identity to SEQ ID NO: 4…”
The instant specification teaches that the invention is drawn to a VEGF dimer linked to a column. The VEGF dimer/linked column is employed to separate soluble fms-like tyrosine kinase-1 (sFLt-1) from blood (abstract and paras 0004-0014). The specification teaches SEQ ID NO: 1 as human full length VEGF-A (232 amino acid residues; para 0036).
The specification teaches wherein the first VEGF molecule of the column has at least 50% amino acid sequence identity to SEQ ID NO:3 and wherein the second VEGF molecule has at least 50% amino acid sequence identity to SEQ ID NO: 4 (paras 0074-0075). However, there is no teaching how to make a variant VEGF having at least 50% sequence identity to the recited SEQ ID Nos that is specific enough to isolate sFLt-1 from blood.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through establishment of a structure-function correlation (show a structure is correlated with the function) OR through a sufficient description of a representative number of species (show a representative number of species that have the function. There must be enough species that are representative of the full breadth of the genus).
Regarding structure-function correlation: The instant claims encompass a genus of VEGF dimer molecules proteins having at least 50% sequence identity to instant SEQ ID NO:3 and instant SEQ ID NO:4.
Instant SEQ ID NO: 3 comprises 167 amino acid residues. A VEGF protein having at least 50% sequence identity means about 83 amino acid residues can be altered. This would include amino acid residue additions, substitutions, insertions and/or deletions.
Instant SEQ ID NO: 4 comprises 170 amino acid residues. A VEGF protein having at least 50% sequence identity means about 85 amino acid residues can be altered. This would include amino acid residue additions, substitutions, insertions and/or deletions.
The artisan would need to know which regions of SEQ ID NO:3 and SEQ ID NO:4 that are responsible for the interactions. The specification does not teach which amino acid residues that are tolerant to change and the nature and extent of changes that can be made in these positions when compared to wildtype SEQ ID NO:3 and SEQ ID NO:4. The specification fails to provide Written Description for randomly selected changes in the disclosed sequences, which would afford a protein having activity comparable to the one disclosed.
The art evidences that the problem of predicting protein structure from sequence data and in turn utilizing predicted structural determinations to ascertain functional aspects of the protein is extremely complex. Even if an active or binding site were identified in the specification, they may not be sufficient, as the ordinary artisan would immediately recognize that an active or binding site must assume the proper three-dimensional configuration to be active, which conformation is dependent upon surrounding residues; therefore substitution of non-essential residues can often destroy activity.
Fenton et al. teach that while it is well known that most substitutions at conserved amino acid positions (which they call “toggle” switches) abolish function, it is also true that substitutions at non-conserved positions (which they call “rheostat” positions) are equally capable of affecting protein function. They conclude that substitutions at rheostat positions have highly unpredictable outcomes on the activities and specificities of protein-based drugs (Fenton et al. Rheostat positions: A new classification of protein positions relevant to pharmacogenomics Medicinal Chemistry Research 29:1133-1146; 2020).
Bhattacharya et al. state that the range of possible effects of even single nucleotide variations at the protein level are significantly greater than currently assumed by existing software prediction methods, and that correct prediction of consequences remains a significant challenge (p. 18) (Bhattacharya et al. Impact of genetic variation on three dimensional structure and function of proteins PLoS ONE 12(3): e0171355; 2017).
In addition, when multiple mutations are introduced, there is even less predictability. As the number of modified sites increases, the number of possible variants, and hence the degree of experimentation required, increases exponentially. As plural substitutions are introduced, their interactions with each other and their effects on the structure and function of the protein become progressively less predictable. For evidence thereof, see Guo et al., who state that the effects of mutations on protein function are largely additive (page 9207, left column, full paragraph 2)(Guo et al. Protein tolerance to random amino acid change. PNAS USA 101(25):9205-10; 2004).
Regarding a representative number of species: the instant specification fails to describe a representative number of species to provide adequate written description of the claimed genus as per MPEP § 2163. There must be enough species that are representative of the full breadth of the genus.
The specification teaches 1 species of a variant VEGF dimer wherein the first molecule comprises a VEGF lacking the N-terminal terminal sequence-linker-second VEGF molecule lacking the N-terminal signal peptide (scVEGF165)(Example 1). One VEGF species is not representative of the claimed genus which encompasses VEGF dimers comprising numerous individual and combinational substitutions, deletions and/or additions with the biological function of specifically binding to sFLt-1. The scope of the claims include numerous structural variants, and the genus is highly variant because a significant number of structural differences between genus members is permitted.
The level of skill and knowledge in the art is such that one of ordinary skill would not be able to identify without further testing which of those molecules have the claimed activity. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. The molecule itself is required. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. In Fiddes v. Baird, 30 USPQ2d 1481, 1483).
One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483 (BPAI 1993). In Fiddes, claims directed to mammalian FGF's were found to be unpatentable due to lack of written description for that broad class. The specification provided only the bovine sequence.
Accordingly, it is deemed that the instant specification fails to provide adequate written description for the genus of the claims and does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-7, 10, 18-23, 26 and 27 are rejected under 35 U.S.C. 102 (a1) and 35 U.S.C. 102 (a2) as being anticipated by Ferrera et al. (US Patent 5,332,671; published July 26, 1994).
Ferrera et al. teach DNA encoding vascular endothelial growth factor (VEGF) and recombinant methods of making VEGF (abstract; column 2, line 61-column 3, line 1 and Figures 1, 2). Ferrera et al. teach a sequence that is 99.1% identical to instant SEQ ID NO:3 and 97.4% identical to instant SEQ ID NO:4. Ferrera et al. teach that the sequences comprise 197 amino acid residues. See below, Sequence search result A and Sequence search result B, respectively (applies to claims 2, 6, 7, 21-23 and 27). Ferrera et al. teach that VEGF can be recombinantly produced in eukaryotic cells (column 11, lines 22-25 and claims)(applies to claims 3 and 18). Proteins such as VEGF that are recombinantly produced in eukaryotic cells, are post-translationally modified. These modifications include wherein the N-terminal signal peptide is cleaved to yield the mature, functional protein (applies to claims 5 and 20).
Ferrera et al. teach since VEGF tends to aggregate into dimers, it is within the scope hereof to provide hetero- and homodimers, wherein one or both subunits are variants. Where both subunits are variants, the changes in amino acid sequence can be the same or different for each subunit chain (applies to claim 1). Ferrera et al. teach heterodimers are readily produced by co-transforming host cells with DNA encoding both subunits and, if necessary, purifying the desired heterodimer, or by separately synthesizing the subunits, dissociating the subunits (e.g., by treatment with a chaotropic agent such as urea, guanidine hydrochloride, or the like), mixing the dissociated subunits, and then reassociating the subunits by dialyzing away the chaotropic agent (column 10, lines 18-32)(applies to claims 1, 4, 19).
Ferrera et al. teach crosslinking the VEGF to a water-insoluble support matrix (applies to claim 1). Ferrera et al. teach commonly used crosslinking agents include, e.g., 1,1-bis(diazoacetyl)-2-phenylethane, glutaraldehyde, N-hydroxysuccinimide esters, for example, esters with 4-azidosalicylic acid, homobifunctional imidoesters, including disuccinimidyl esters such as 3,3'-dithiobis(succinimidylpropionate), and bifunctional maleimides such as bis-N-maleimido-1,8-octane. Derivatizing agents such as methyl-3-[(p-azidophenyl)dithio]propioimidate yield photoactivatable intermediates that are capable of forming crosslinks in the presence of light. Alternatively, reactive water-insoluble matrices such as cyanogen bromide-activated carbohydrates and the reactive substrates described in U.S. Pat. Nos. 3,969,287; 3,691,016; 4,195,128; 4,247,642; 4,229,537; and 4,330,440 are employed for protein immobilization (column 7, lines 20-38)(i.e. covalent bond, applies to claims 1, 10 and 26).
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1, 8, 9, 24 and 25 are rejected under 35 U.S.C. 103 as being unpatentable over Ferrera et al. (US Patent 5,332,671; published July 26, 1994) in view of Cochran et al. (US 2018/0369334; published Dec 27, 2018).
Ferrera et al. teach DNA encoding vascular endothelial growth factor (VEGF) and recombinant methods of making VEGF (abstract; column 2, line 61-column 3, line 1 and Figures 1, 2). Ferrera et al. teach a sequence that is 99.1% identical to instant SEQ ID NO:3 and 97.4% identical to instant SEQ ID NO:4. The sequences comprise 197 amino acid residues. See below, Sequence search result A and Sequence search result B, respectively (applies to claim 2). Ferrera et al. teach that VEGF can be recombinantly produced in eukaryotic cells (column 11, lines 22-25 and claims). Ferrera et al. teach since VEGF tends to aggregate into dimers, it is within the scope hereof to provide hetero- and homodimers, wherein one or both subunits are variants. Where both subunits are variants, the changes in amino acid sequence can be the same or different for each subunit chain. Heterodimers are readily produced by co-transforming host cells with DNA encoding both subunits and, if necessary, purifying the desired heterodimer, or by separately synthesizing the subunits, dissociating the subunits (e.g., by treatment with a chaotropic agent such as urea, guanidine hydrochloride, or the like), mixing the dissociated subunits, and then reassociating the subunits by dialyzing away the chaotropic agent (column 10, lines 18-32)(applies to claim 1). Ferrera et al. teach derivatization with bifunctional agents is useful for crosslinking the VEGF to a water-insoluble support matrix (applies to claim 1). Ferrera et al. teach commonly used crosslinking agents include, e.g., 1,1-bis(diazoacetyl)-2-phenylethane, glutaraldehyde, N-hydroxysuccinimide esters, for example, esters with 4-azidosalicylic acid, homobifunctional imidoesters, including disuccinimidyl esters such as 3,3'-dithiobis(succinimidylpropionate), and bifunctional maleimides such as bis-N-maleimido-1,8-octane. Derivatizing agents such as methyl-3-[(p-azidophenyl)dithio]propioimidate yield photoactivatable intermediates that are capable of forming crosslinks in the presence of light. Alternatively, reactive water-insoluble matrices such as cyanogen bromide-activated carbohydrates and the reactive substrates described in U.S. Pat. Nos. 3,969,287; 3,691,016; 4,195,128; 4,247,642; 4,229,537; and 4,330,440 are employed for protein immobilization (column 7, lines 20-38)(i.e. covalent bond, applies to claim 1).
Ferrera et al. teach recombinantly or chemically synthesizing VEGF. Ferrera et al. teach covalently crosslinking the VEGF to a water-insoluble support matrix. Ferrera et al. teach since VEGF tends to aggregate into dimers, it is within the scope hereof to provide hetero- and homodimers.
Ferrera et al. do not teach wherein the hetero- or the homodimers of VEGF are linked by a linker.
Cochran et al. teach VEGF polypeptides comprising a first VEGF monomer joined to a second VEGF monomer by a peptide linker. Cochran et al. teach wherein the linker has a length of 10 to 30 amino acids (paras 0002-0012 and 0106-0107)(applies to claims 8, 9, 24 and 25).
It would have been obvious for one of ordinary skill in the art before the effective filling date to modify a column comprising a VEGF dimer molecule comprising a first and a second VEGF molecule, as taught by Ferrera et al., by adding a linker between the first and the second molecule, as taught by Cochran et al. One of ordinary skill in the art before the effective filing date, would have been motivated to make such modifications and expect success because linkers are known in the art to join various domains, subunits, etc. They can also improve protein stability, enhance biological activity and increase expression yields.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to REGINA M DEBERRY whose telephone number is (571)272-0882. The examiner can normally be reached M-F 9:00-6:30 pm (alt Fri).
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Joanne Hama can be reached at 571-272-2911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/R.M.D/Examiner,ArtUnit1647
1/21/2026
/BRIDGET E BUNNER/Primary Examiner, Art Unit 1647
SEQUENCE SEARCH RESULT A
This page gives you Search Results detail for the Application 17906730 and Search Result 20251203_102149_us-17-906-730-3.pct85.rai
Title: US-17-906-730-3
Perfect score: 946
Sequence: 1 ASAPMAEGGGQNHHEVVKFM..........CKARQLELNERTCRCDKPRR 167
%
Result Query Filing
No. Score Match Length ID Date Dups Description
------------------------------------------------------------------------------
1 939 99.3 191 US-07-389-722-4 1989-08-04 151 PRODUCTION OF VASCULAR ENDOTHELIAL CELL
ALIGNMENTS
RESULT 1
US-07-389-722-4
(NOTE: this sequence has 151 duplicates in the database searched.
See complete list at the end of this report)
Sequence 4, US/07389722
Patent No. 5332671
GENERAL INFORMATION
APPLICANT: FERRARA, NAPOLEONE;LEUNG, DAVID W.H.
TITLE OF INVENTION: PRODUCTION OF VASCULAR ENDOTHELIAL CELL
CURRENT APPLICATION NUMBER: US/07/389,722
CURRENT FILING DATE: 04-AUG-1989
PRIOR APPLICATION NUMBER: 369,424
PRIOR FILING DATE: 21-JUN-1989
PRIOR APPLICATION NUMBER: 351,117
PRIOR FILING DATE: 12-MAY-1989
NUMBER OF SEQ ID NOS: 15
SEQ ID NO 4
LENGTH: 191
TYPE: PRT
Query Match 99.3%; Score 939; Length 191;
Best Local Similarity 99.4%;
Matches 165; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 2 SAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGG 61
:|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 26 AAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGG 85
Qy 62 CCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQENPCGP 121
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 86 CCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQENPCGP 145
Qy 122 CSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR 167
||||||||||||||||||||||||||||||||||||||||||||||
Db 146 CSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR 191
SEQUENCE SEARCH RESULT B
This page gives you Search Results detail for the Application 17906730 and Search Result 20251203_102149_us-17-906-730-4.pct85.rai
Title: US-17-906-730-4
Perfect score: 963
Sequence: 1 TRAPMAEGGGQNHHEVVKFM..........RQLELNERTCRCDKPRRGST 170
SUMMARIES
%
Result Query Filing
No. Score Match Length ID Date Dups Description
------------------------------------------------------------------------------
4 938 97.4 191 US-07-389-722-4 1989-08-04 151 PRODUCTION OF VASCULAR ENDOTHELIAL CELL
RESULT 4
US-07-389-722-4
(NOTE: this sequence has 151 duplicates in the database searched.
See complete list at the end of this report)
Sequence 4, US/07389722
Patent No. 5332671
GENERAL INFORMATION
APPLICANT: FERRARA, NAPOLEONE;LEUNG, DAVID W.H.
TITLE OF INVENTION: PRODUCTION OF VASCULAR ENDOTHELIAL CELL
CURRENT APPLICATION NUMBER: US/07/389,722
CURRENT FILING DATE: 04-AUG-1989
PRIOR APPLICATION NUMBER: 369,424
PRIOR FILING DATE: 21-JUN-1989
PRIOR APPLICATION NUMBER: 351,117
PRIOR FILING DATE: 12-MAY-1989
NUMBER OF SEQ ID NOS: 15
SEQ ID NO 4
LENGTH: 191
TYPE: PRT
Query Match 97.4%; Score 938; Length 191;
Best Local Similarity 100.0%;
Matches 165; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 3 APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGC 62
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 27 APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGC 86
Qy 63 CNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQENPCGPC 122
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 87 CNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQENPCGPC 146
Qy 123 SERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR 167
|||||||||||||||||||||||||||||||||||||||||||||
Db 147 SERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR 191