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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 04/15/2026 has been entered.
Priority
This application is a 371 of PCT/CN2021/071497 filed 01/13/2021. Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged.
Acknowledgment is made of applicant’s claim for foreign priority under 35 U.S.C. 119 (a)-(d) based on CN 202010036519.0 filed 01/14/2020 and CN 202010036500.6 filed 01/14/2020. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Status of the Claims
Claims 1-6, 9-15 and 19-25 are pending. Claims 1 and 3 are amended. Claims 9-13 and 19-25 are withdrawn. Claims 7, 8 and 26 are cancelled.
Claims 1-6, 14 and 15 (claim set filed 03/11/2026) are examined on the merits herein.
Withdrawal of Rejections
The response and amendment filed on 03/11/2026 are acknowledged. All of the amendment and arguments have been thoroughly reviewed and considered.
For the purposes of clarity of the record, the reasons for the Examiner's withdrawal and/or maintaining if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner's response to arguments section.
The previous claims 1-8, 14, 15 and 26 rejections under 35 U.S.C. 112(a) have been withdrawn necessitated by amendment of claim 1.
New Rejections
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 6 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 6 recites the limitation "the catalytic site A" in line 2. There is insufficient antecedent basis for this limitation in the claim. Claim 6 depends on claim 5, depending on claim 1. Neither claim 5, not claim 1 recite “a catalytic site A”. It is not clear what catalytic site claim 6 is referring to. The scope and boundaries of claim 6 are not certain making claim 6 indefinite.
Maintained/Modified Rejections
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 1-6, 14 and 15 are rejected under 35 U.S.C. 103 as being unpatentable over GenBank 1 (GenBank KMT22110.1, 2015 [retrieved on 01/13/2025]. Retrieved from the Internet:< isochorismatase-like protein [Clostridium cylindrosporum DSM 605] - Protein - NCBI>) in view of Rabinowitz (Rabinowitz and Pricer J. Biol. Chem., 1956, 218, 189-199 on record in IDS), GenBank 2 (GenBank AND39904.1, 2016 [retrieved on 11/30/2025]. Retrieved from the Internet <allantoinase [Cytobacillus oceanisediminis 2691] - Protein - NCBI>) and Percudani (WO 2007052326 A2).
Regarding claim 1, GenBank 1 provides sequence for isochorismatase-like protein from Clostridium cylindrosporum DSM 605 genome. The sequence from GenBank 1 is 100% identical to instant SEQ ID NO:1 of the polypeptide A which is 4-ureido-5-carboxyimidazole amide hydrolase as described in the specification (paragraph 0070). Since GenBank 1 teaches polypeptide with the claimed sequence, this polypeptide will necessarily possess 4-ureido-5-carboxyimidazole amide hydrolase activity. MPEP 2112.01 states: “Products of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present.”
GenBank 1 does not teach a polypeptide B with SEQ ID NO: 103 and a composition comprising polypeptide A and polypeptide B.
Rabinowitz teaches purine fermentation by Clostridium cylindrosporum (Title). Rabinowitz describes degradation of xanthine to glycine, formic acid and ammonia by extracts of Clostridium cylindrosporum (p. 189, 1st paragraph and p. 190 – scheme). Rabinowitz mentions that another biochemical transformation of xanthine is to uric acid (p. 198, 2nd paragraph). Rabinowitz discloses that xanthine incubated with Clostridium cylindrosporum extracts is converted to 4-ureido-5- carboxyimidazole carboxylic acid and in vitro incubation of 4-ureido-5-carboxyimidazole carboxylic acid with the extracts of Clostridium cylindrosporum results in its degradation (hydrolysis) to 4-amino-5- imidazole carboxylic acid (p. 196, 3rd paragraph, pp. 198-199 - Summary). Rabinowitz mentions that hydrolysis to 4-ureido-5-carboxyimidazole carboxylic acid is similar to conversion of allantoin to allantoic acid (p. 198, 2nd paragraph). Thus, Rabinowitz indicated presence of enzymes in the xanthine degradation pathway catalyzing reaction of formation of 4-ureido-5-carboxyimidazole carboxylic acid from xanthine corresponding to reaction of instant polypeptide A and reaction of hydrolysis of 4-ureido-5-carboxyimidazole carboxylic acid to 4-amino-5- imidazole carboxylic acid corresponding to reaction of instant polypeptide B (p. 190, Scheme).
GenBank 2 teaches the sequence for allantoinase from Cytobacillus oceanisediminis 2691. That polypeptide has 100% identity to instant SEQ ID NO: 103 which is xanthine amide hydrolase as described in the specification (paragraph 0172). Since GenBank 2 teaches polypeptide with the claimed sequence, this polypeptide will necessarily possess xanthine amide hydrolase activity producing 4-ureido-5-carboxyimidazole carboxylic acid from xanthine.
Percudani teaches a pharmaceutical composition for treating uric acid related disorders by modulating uric acid conversion to allantoin (Abstract). Percudani describes oxidation of xanthine in the purine degradation pathway to uric acid by xanthine oxidase. The uric acid can be further oxidized to allantoin by urate oxidase in most mammals but not in humans. Humans do not have enzyme degrading uric acid and high level of uric acid (hyperuricemia) can lead to such condition as gout when crystals accumulate in joints (p. 1, lines 7-19). Percudani discloses two specific enzymes which can degrade uric acid to allantoin and describes that administration of these polypeptides together with urate oxidase can provide treatment of hyperuricemia (p. 3, lines 9-12, 22- 25). Percudani mentions that administration of these enzymes together provides more effective and safe treatment of hyperuricemia (p. 3, lines 23-25). Percudani teaches pharmaceutical composition comprising at least one of these polypeptides for treatment of uric acid related disorders (p. 4, lines 28-29).
First, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to follow teaching of Rabinowitz and identify the polypeptide of GenBank 1 teaching isolated from Clostridium cylindrosporum as the enzyme of the xanthine degradation pathway and confirm its enzymatic activity in vitro by hydrolysis of 4-ureido-5-carboxyimidazole carboxylic acid. One would have been motivated to do so since Rabinowitz identified intermediates in the xanthine degradation pathway in Clostridium cylindrosporum and measured hydrolysis of 4-ureido-5- carboxyimidazole carboxylic acid which is the inherent functional property of the polypeptide from GenBank 1 teaching isolated from the same species. A skilled artisan would have reasonably expected success in that because GenBank 1 and Rabinowitz teach the enzyme with the same activity.
Second, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to identify the polypeptide of GenBank 2 teaching as another enzyme of the xanthine degradation pathway, xanthine amide hydrolase, preceding the 4-ureido-5-carboxyimidazole amide hydrolase in the xanthine degradation pathway as was shown by Rabinowitz. One would have been motivated to do so since Rabinowitz identified intermediates in the xanthine degradation pathway and predicted presence of xanthine amide hydrolase producing in 4-ureido-5-carboxyimidazole carboxylic acid and having reaction similar to allantoin conversion to allantoic acid and xanthine amide hydrolase activity is the inherent functional property of the polypeptide from GenBank 2 identical to claimed polypeptide B and this polypeptide is referred as allantoinase in GenBank 2. A skilled artisan would have reasonably expected success in this combination because GenBank 1, GenBank 2 and Rabinowitz teach the enzymes with the same activities, GenBank 1 and GenBank 2 provided the sequences and Rabinowitz identified pathway and intermediates and described the instructions for the enzymatic reactions.
Third, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to follow teaching of Percudani and prepare pharmaceutical composition for treatment of uric acid related disorders such as gout as described by Percudani with the polypeptides from GenBank 1 and GenBank 2 which are involved in degradation of xanthine as taught by Rabinowitz. One would have been motivated to do so since GenBank 1 provides the sequence of the polypeptide catalyzing hydrolysis of 4-ureido-5-carboxyimidazole carboxylic acid, GenBank 2 provides the sequence of the polypeptide catalyzing production of 4-ureido-5-carboxyimidazole carboxylic acid from xanthine, Rabinowitz showed these activities to be involved in the degradation of xanthine and Percudani teaches that conversion of xanthine to uric acid leads to disorders such as gout and can be treated with removal of uric acid and hence hydrolysis of xanthine by the pathway described by Rabinowitz will decrease production of uric acid. Additionally, Percudani teaches that administration of the composition comprising three enzymes of the same pathway together leads to more efficient and safe treatment of hyperuricemia providing motivation to include both polypeptides of GenBank 1 and GenBank 2 in the composition to increase its efficacy. A skilled artisan would have reasonably expected success in this combination because GenBank 1, GenBank 2, Rabinowitz and Percudani teach enzymes involved in xanthine degradation.
Thus, GenBank 1, Rabinowitz, GenBank 2 and Percudani teachings render claim 1 obvious.
Regarding claims 2-6, claim 2 is directed to a catalytic site of the polypeptide A and claim 5 is directed to the binding site of the polypeptide A. Claims 2 and 5 recite the properties of the structure which is the polypeptide A with the SEQ ID NO:1. Claims 3 and 4 recite further limitation of claim 2 property and claim 6 recites further limitation for claim 5 property. Pursuant to MPEP 2112.01(I), where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). Therefore, since the polypeptide of GenBank 1 teaching has the claimed structure, the polypeptide of the prior art inherently has property of a catalytic site including catalytic triads close to each other in spatial conformation further comprising a divalent metal ion and further comprising four amino acid residues coordinated with metal ion and the polypeptide of GenBank 1 teaching inherently has property of a binding site with the defined amino acid residues close to each other and the distance between the catalytic site and the binding site of not more than 5 angstroms. Thus, GenBank 1, Rabinowitz, GenBank 2 and Percudani teachings render claims 2-6 obvious.
Regarding claims 14 and 15, as described above, Percudani teaches a pharmaceutical composition for treating uric acid related disorders such as gout. Percudani discloses that humans do not have enzyme degrading uric acid and high level of uric acid (hyperuricemia) can lead to such condition as gout when crystals accumulate in joints (p. 1, lines 7-19). Percudani describes that uric acid is produced in purine degradation pathway from xanthine. Percudani discloses pharmaceutical composition comprising two specific enzymes which can degrade uric acid to allantoin and describes that administration of these polypeptides together with urate oxidase can provide treatment of hyperuricemia (p. 3, lines 9-12, 22- 25).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to prepare pharmaceutical composition for treatment of gout as described by Percudani with the polypeptides from GenBank 1 and GenBank 2 which are involved in degradation of xanthine as taught by Rabinowitz. One would have been motivated to do so since GenBank 1 and GenBank 2 provide the sequences of hydrolases involved in degradation of xanthine as taught by Rabinowitz and Percudani teaches that conversion of xanthine to uric acid leads to disorders such as gout and hence hydrolysis of xanthine by the pathway described by Rabinowitz will decrease production of uric acid and prevent or treat gout disease. A skilled artisan would have reasonably expected success in this combination because GenBank 1, GenBank 2, Rabinowitz and Percudani teach enzymes involved in xanthine degradation. Thus, GenBank 1, Rabinowitz, GenBank 2 and Percudani teachings render claims 14 and 15 obvious.
Response to Arguments
Applicant's arguments filed 03/11/2026 have been fully considered but they are not persuasive.
Applicant argues (addressing p. 6-9 of the Remarks) that combination of GenBank 1, Rabinowitz and GenBank 2 fails to teach or suggest the polypeptide composition of claim 1 and that there is no teaching or suggestion that would lead one of ordinary skill in the art to combine GenBank 1 and GenBank 2. Applicant further argues that Rabinowitz teaching does not provide connection between similar reactions of the hydrolysis to 4-ureido-5-imidazolecarboxylic acid and addition of another enzyme, xanthine amide hydrolase. These arguments are not persuasive because:
Current rejection is based on combination of prior art of GenBank 1, Rabinowitz, GenBank 2 and Percudani as described above. Although GenBank 1, Rabinowitz and GenBank 2 do not teach composition of polypeptides A and B, GenBank 1 and GenBank 2 teach sequences of polypeptides A and B and Rabinowitz teaches the xanthine degradation pathway including reactions catalyzed by the polypeptides A and B (p. 190, Scheme, pp. 198-199 – Summary). Percudani teaches composition comprising enzymes degrading uric acid, the product of xanthine oxidation, high levels of which result in hyperuricemia and lead to such condition as gout (p. 1, lines 7-19, p. 4, lines 28-29). That provides motivation to prepare composition for prevention or treatment of hyperuricemia related disorders such as gout that can reduce the amount of xanthine preventing it from being degraded to uric acid. Since Rabinowitz teaches pathway of xanthine hydrolysis and its intermediates suggesting presence of hydrolases for the specific steps of the pathway and GenBank 1 and GenBank 2 provide sequences for such enzymes, it provides motivation to include these hydrolases in the composition for prevention or treatment of hyperuricemia. Besides, Percudani mentions that administration of several enzymes of the same pathway together provides more effective and safe treatment of hyperuricemia (p. 3, lines 23-25) and that suggests to include both polypeptides of GenBank 1 and GenBank 2 in the composition to increase its efficacy in prevention or treatment of uric acid related disorders such as gout.
Therefore, the 35 U.S.C. 103 rejection is maintained and modified.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-6, 14 and 15 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 18 and 19 of copending Application No. 17/793,014 in view of in view of GenBank 1 (GenBank KMT22110.1, 2015 [retrieved on 01/13/2025]. Retrieved from the Internet:< isochorismataselike protein [Clostridium cylindrosporum DSM 605] - Protein - NCBI>) and Rabinowitz (Rabinowitz and Pricer J. Biol. Chem., 1956, 218, 189-199 on record in IDS).
Claim 1 is directed to a polypeptide composition comprising polypeptide A and polypeptide B. Claims 14 and 15 are directed to a pharmaceutical composition comprising polypeptide composition of claim 1 used for prevention, intervention and/or treatment of gout.
Regarding claims 1, 14 and 15, reference claims 18 and 19 teach methods for treating gout comprising the polypeptide functional variant of amino acid sequence with SEQ ID NO:1 with xanthine amide hydrolase activity. The SEQ ID NO: 1 of reference application is 100% identical to instant SEQ ID NO:103 for polypeptide B. Although the reference application teaches method of treatment, it would be obvious to one of ordinary skill in the art that the method of treatment requires the pharmaceutical composition.
The reference claims 18 and 19 do not teach the polypeptide A.
GenBank 1 teaches polypeptide from Clostridium cylindrosporum DSM 605 genome 100% identical to instant SEQ ID NO:1 of the instant polypeptide A. Since the Clostridium cylindrosporum polypeptide of GenBank 1 teaching has the identical structure to the claimed polypeptide A with SEQ ID NO:1, the polypeptide of the prior art inherently possesses the functional property, i.e. 4-ureido-5-carboxyimidazole amide hydrolase activity.
Rabinowitz teaches that xanthine incubated with Clostridium cylindrosporum extracts is converted to 4-ureido-5-carboxyimidazole carboxylic acid which is hydrolyzed to 4-amino-5-imidazole carboxylic acid (p. 196, 3rd paragraph, pp. 198-199 - Summary) and thus describes sequential reactions of the claimed polypeptide B with xanthine amide hydrolase activity and polypeptide A with 4-ureido-5- carboxyimidazole amide hydrolase activity in Clostridium cylindrosporum extracts.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to add polypeptide from GenBank 1 teaching to the pharmaceutical composition for treatment of gout based on method taught in the reference application. One would have been motivated to do so since GenBank 1 provides the sequence of the polypeptide catalyzing hydrolysis of 4- ureido-5-carboxyimidazole carboxylic acid and the reference application teaches method comprising polypeptide of the same pathway hydrolyzing xanthine as shown by Rabinowitz and resulting in production of 4-ureido-5-carboxyimidazole carboxylic acid and hence the combination of polypeptides will decrease production of uric acid from xanthine resulting in prevention or treatment of gout. A skilled artisan would have reasonably expected success in this combination because the reference application, GenBank 1 and Rabinowitz teach enzymes involved in xanthine degradation. Thus, combination of the reference claims 18 and 19, GenBank 1 and Rabinowitz renders claims 1, 14 and 15 obvious.
Regarding claims 2-6, claim 2 is directed to a catalytic site of the polypeptide A and claim 5 is directed to the binding site of the polypeptide A. Claims 2 and 5 recite the properties of the structure which is the polypeptide A with the SEQ ID NO:1. Claims 3 and 4 recite further limitation of claim 2 property and claim 6 recites further limitation for claim 5 property. Pursuant to MPEP 2112.01(I), where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). Therefore, since the polypeptide of GenBank 1 teaching has the claimed structure, the polypeptide of the prior art inherently has property of a catalytic site including catalytic triads close to each other in spatial conformation further comprising a divalent metal ion and further comprising four amino acid residues coordinated with metal ion and the polypeptide of GenBank 1 teaching inherently has property of a binding site with the defined amino acid residues close to each other and the distance between the catalytic site and the binding site of not more than 5 angstroms. Thus, reference claims 18 and 19, GenBank 1 and Rabinowitz teachings render claims 2-6 obvious.
Therefore, since instant claims 1-6, 14 and 15 encompass the subject matter of the reference claims 18 and 19, they are rejected under obviousness double patenting.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant states (addressing p. 9 of the Remarks) that this is a provisional rejection and both applications are still pending and that the double patenting rejection will be addressed upon indication of allowability if necessary. The Applicant comment is acknowledged. The double patenting rejection is maintained and modified taking into consideration amendment of claims of both applications.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to LIOUBOV G KOROTCHKINA whose telephone number is (571)270-0911. The examiner can normally be reached Monday-Friday: 8:00-5:30.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Sharmila G Landau can be reached at (571)272-0614. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/L.G.K./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
