DETAILED CORRESPONDENCE
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1-5, 9, 10, 13-17, 21, 25, 26 and 28 are pending in the application.
Applicant’s amendment to the claims, filed October 15, 2025, is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Applicant’s remarks and declaration under 37 CFR 1.132 (hereafter “Second Suzuki Declaration”) filed October 15, 2025 in response to the non-final rejection mailed April 17, 2025 have been fully considered.
Restriction/Election
In response to a requirement for restriction/election mailed September 3, 2021, applicant elected without traverse:
Group II, corresponding to pending claims 13-17, 21, 25, 26, and 28;
species A), pyruvate kinase (PK) in claims 15 and 25; and
species AA), pyruvate orthophosphate dikinase (PPDK) in claim 17.
Claims 1-5, 9, and 10 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on September 3, 2021.
Claims 13-17, 21, 25, 26 and 28 are being examined on the merits with claims 15, 17, and 25 being examined only to the extent the claims read on the elected subject matter. In the interest of clarity, it is noted that a rejection set forth below may be directed to a non-elected species, which has yet to be searched and examined on the merits because the cited prior art was identified during a search and examination of the elected species as set forth above.
Claim Rejections - 35 USC § 103
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 rejection of claims 13-17, 21, 25, 26, and 28 under 35 U.S.C. 103 as being unpatentable over Hansen et al. (“ATP bioluminescence – for kitchen hygiene and cleaning control of surgical instruments”, Int. J. Infect. Contr. 4:1, 2008, 4 pages; cited on Form PTO-892 mailed on November 18, 2022; hereafter “Hansen-1”) in view of Strategic Diagnostics Incorporated (“The Lumitester PD 10-N and LuciPac W for Hygiene Monitoring”, 2007, 2 pages; cited on Form PTO-892 mailed on March 15, 2024; hereafter “Lumitester PD 10”) and U.S. Patent No. 5,891,659 (cited on Form PTO-892 mailed on March 15, 2024) is withdrawn in view of the amendment to claims 13, 14, and 26 to recite “wherein adenosine monophosphate (AMP) is not added to the reaction mixture” and the evidence provided by Second Suzuki Declaration. U.S. Patent No. 5,891,659 teaches measuring ADP luminescence in a reaction comprising pyruvate kinase (column 9, bottom to column 10, top) and teaches the pyruvate kinase is made by Boehringer-Mannheim GmbH (column 13, top). Second Suzuki Declaration provides evidence that commercial sources of pyruvate kinase (such as pyruvate kinase made by Boehringer-Mannheim GmbH) are obtained from rabbit muscle and comprise AMP. By the amendment to claims 13, 14, and 26 to recite “wherein adenosine monophosphate (AMP) is not added to the reaction mixture,” the claims exclude commercial sources of pyruvate kinase obtained from rabbit muscle and comprising AMP.
The rejection of claims 13, 14, 21, 26, and 28 under 35 U.S.C. 103 as being unpatentable over Hansen-1 in view of Lumitester PD-10 and Satoh et al. (Biosci. Biotechnol. Biochem. 68:1216-1220, 2004; cited on Form PTO-892 mailed on March 15, 2024; hereafter “Satoh”) is withdrawn in view of the amendment to claims 13, 14, and 26 to recite “wherein adenosine monophosphate (AMP) is not added to the reaction mixture.” Satoh teaches a reaction mixture comprising AMP (p. 1217, column 2, top) and the combination of Hansen-1, Lumitester PD-10, and Satoh does not teach or suggest “wherein adenosine monophosphate (AMP) is not added to the reaction mixture.”
Claims 13-17, 21, 25, 26, and 28 are newly rejected under 35 U.S.C. 103 as being unpatentable over Hansen-1, Lumitester PD 10, U.S. Patent No. 5,891,659, Murcott et al. (Eur. J. Biochem. 198:513-519, 1991; cited on the attached Form PTO-892; hereafter “Murcott”), and Sakai et al. (J. Biochem. 99:1157-1167, 1986; cited on the attached Form PTO-892; hereafter “Sakai”). The instant rejection is necessitated by the amendment to recite “wherein adenosine monophosphate (AMP) is not added to the reaction mixture” in claims 13, 14, and 26.
Hansen-1 teaches that reprocessing procedures for medical devices is often monitored by determination of residual blood on instruments after reprocessing, however, described methods for detection of blood are too cumbersome to be performed routinely at reprocessing sites for medical devices (p. 1, column 1). Hansen-1 teaches ATP is a constituent of all living cells and teaches ATP bioluminescence assay to verify success of cleaning in reprocessing of medical devices (p. 1, column 2) and for quality control of reprocessing of surgical instruments (p. 3, column 1). More specifically, Hansen-1 discloses using ATP bioluminescence assay to check endoscope reprocessing (p. 2, column 2) and to verify the cleaning of contaminated surgical instruments in the context of validation of washer-disinfectors (p. 3, Figure 4 and column 2). Hansen-1 teaches Lumitester PD 10 for measuring ATP bioluminescence (p. 2, column 2, bottom).
Lumitester PD 10 teaches that because ATP is present in all living cells, it is an indicator of biological contamination (p. 1, middle column). Lumitester PD 10 teaches that the Lumitester takes hygiene monitoring one step further by detecting both ATP and AMP, which improves sensitivity (p. 1, column 1 and middle paragraph). Lumitester PD 10 teaches measuring ATP and AMP bioluminescence by means of an enzyme reaction including pyruvate orthophosphate dikinase, luciferin, luciferase, and Mg2+ (p. 2, bottom). Lumitester PD 10 cites to U.S. Patent No. 5,891,659 (p. 2, bottom).
Hansen-1 and Lumitester PD 10 do not teach an enzyme that catalyzes a reaction that produces ATP from ADP.
U.S. Patent No. 5,891,659 teaches that, in addition to measuring AMP bioluminescence (column 8), ADP luminescence can also be measured, wherein ADP is converted to ATP in a reaction comprising pyruvate kinase (columns 9, bottom to column 10, top). According to U.S. Patent No. 5,891,659, the disclosed methods have high sensitivity and high accuracy (column 3, bottom; column 10, bottom).
U.S. Patent No. 5,891,659 teaches pyruvate kinase made by Boehringer-Mannheim GmbH. In view of evidence provided by Second Suzuki Declaration, pyruvate kinase made by Boehringer-Mannheim GmbH is obtained from rabbit muscle, comprises AMP, and is thus excluded from claims 13, 14, and 26 by the recitation of “wherein adenosine monophosphate (AMP) is not added to the reaction mixture.”
However, pyruvate kinase obtained from a source other than rabbit muscle was well-known in the prior art before the effective filing date, e.g., Murcott teaches purified pyruvate kinase from yeast (p. 513, abstract) and Sakai teaches purified pyruvate kinase from Bacillus stearothermophilus (p. 1157, abstract). Also, U.S. Patent No. 5,891,659 teaches acetate kinase or creatine kinase may be used in place of pyruvate kinase (column 10, lines 25-27).
In view of Hansen-1, Lumitester PD 10, U.S. Patent No. 5,891,659, Murcott, and Sakai, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify Hansen-1 to measure ADP luminescence with yeast pyruvate kinase, Bacillus stearothermophilus pyruvate kinase, acetate kinase, or creatine kinase.
One would have been motivated to and would have expected success to measure ADP luminescence because Lumitester PD 10 teaches that measuring AMP and ATP bioluminescence has the effect of increasing sensitivity and cites to U.S. Patent No. 5,891,659, which teaches that, in addition to measuring AMP and ATP bioluminescence, ADP bioluminescence can be measured and discloses that the methods have high sensitivity and high accuracy.
While U.S. Patent No. 5,891,659 teaches an exemplary pyruvate kinase made by Boehringer-Mannheim GmbH to measure ADP bioluminescence, in view of the teachings of Murcott, Sakai, and U.S. Patent No. 5,891,659, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute pyruvate kinase made by Boehringer-Mannheim GmbH with yeast pyruvate kinase, Bacillus stearothermophilus pyruvate kinase, acetate kinase, or creatine kinase. One of ordinary skill would have expected success and could have substituted pyruvate kinase made by Boehringer-Mannheim GmbH with yeast pyruvate kinase or Bacillus stearothermophilus pyruvate kinase because pyruvate kinase made by Boehringer-Mannheim GmbH, yeast pyruvate kinase, and Bacillus stearothermophilus pyruvate kinase have the same enzymatic activity, i.e., pyruvate kinase enzymatic activity. One of ordinary skill would have expected success and could have substituted pyruvate kinase made by Boehringer-Mannheim GmbH with acetate kinase or creatine kinase because U.S. Patent No. 5,891,659 teaches acetate kinase or creatine kinase may be used in place of pyruvate kinase. One of ordinary skill would have found it obvious to make the substitution of pyruvate kinase made by Boehringer-Mannheim GmbH with yeast pyruvate kinase, Bacillus stearothermophilus pyruvate kinase, acetate kinase, or creatine kinase because, based on the relevant teachings of Murcott, Sakai, and U.S. Patent No. 5,891,659, an ordinarily skilled artisan would have predicted that yeast pyruvate kinase, Bacillus stearothermophilus pyruvate kinase, acetate kinase, or creatine kinase would be equivalent to pyruvate kinase made by Boehringer-Mannheim GmbH in the measurement of ADP bioluminescence.
Therefore, the methods of claims 13-17, 21, 25, 26, and 28 would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
RESPONSE TO REMARKS: Applicant argues that in view of Hansen-1, one of ordinary skill in the art would have used ATP bioluminescence that measures ATP only, and there would have been no motivation to measure ATP and ADP, or ATP, ADP, and AMP.
Applicant’s argument has been fully considered but is not found persuasive. Contrary to the applicant’s position, Lumitester PD 10 as taught by Hansen-1 detects both ATP and AMP. See also Hansen-2 (German Medical Science 2:1-5, 2004; cited on Form PTO-892 mailed on March 15, 2024), which teaches determining ATP and AMP bioluminescence using Lumitester PD 10 (p. 2, column 1, middle). As taught by Lumitester PD 10, getting actionable results from traditional ATP reagents can be difficult and inaccurate, noting that false positives by detection of only ATP are common and detection of both ATP and AMP provides better hygiene monitoring (p. 1, column 1). There is nothing in the prior art of record that discourages from a bioluminescence assay using an enzyme that catalyzes a reaction that produces ATP from ADP for detecting blood contamination on surgical instruments. Rather, given that bioluminescence methods using an enzyme that catalyzes a reaction that produces ATP from ADP have high sensitivity (see U.S. Patent No. 5,891,659), one would have been motivated to modify Hansen-1 according to U.S. Patent No. 5,891,659.
Applicant argues pyruvate kinase taught by U.S. Patent No. 5,891,659 is obtained from muscle and in view of the evidence of the Second Suzuki Declaration, contains contaminating AMP, which would reduce the sensitivity of the emission of light from the reaction mixture in the claimed methods.
Applicant’s argument and Second Suzuki Declaration have been fully considered but are not found persuasive. It is acknowledged that the Second Suzuki Declaration provides evidence that pyruvate kinase from rabbit muscle comprises AMP and the amended claims 13, 14, and 26 require that “adenosine monophosphate (AMP) is not added to the reaction mixture.” However, as stated above, given that U.S. Patent No. 5,891,659 teaches acetate kinase or creatine kinase may be used in place of pyruvate kinase (column 10, lines 25-27) and pyruvate kinases obtained from sources other than muscle were well-known in the prior art before the effective filing date, e.g., purified pyruvate kinase from yeast and purified pyruvate kinase from Bacillus stearothermophilus, it would have been obvious to one of ordinary skill in the art to replace pyruvate kinase made by Boehringer-Mannheim GmbH with acetate kinase, creatine kinase, purified pyruvate kinase from yeast, or purified pyruvate kinase from Bacillus stearothermophilus for measuring ADP bioluminescence. Given that acetate kinase, creatine kinase, purified pyruvate kinase from yeast, and purified pyruvate kinase from Bacillus stearothermophilus are not obtained from muscle, they cannot contain contaminating AMP from muscle.
For these reasons, it is the examiner’s position that the claimed invention would have been prima facie obvious before the effective filing date of the claimed invention.
Claim Rejections - 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.
The rejection of claims 13-17, 21, 25, 26, and 28 on the ground of nonstatutory double patenting as being unpatentable over claims 3-6 of U.S. Patent No. 5,891,659 in view of Hansen-1, Lumitester PD 10, and U.S. Patent No. 5,891,659,
the provisional rejection of claims 13-17, 21, 25, 26, and 28 on the ground of nonstatutory double patenting as being unpatentable over claim 15 of co-pending application 17/799,134 in view of Champiat, D. (US 2008/0014607 A1; cited on Form PTO-892 mailed September 21, 2021; hereafter “Champiat”) and Hansen-1, and
the provisional rejection of Claims 13-17, 21, 25, 26, and 28 on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4, and 7 of co-pending application 18/997,307 in view of Champiat and Hansen-1
are withdrawn in view of the amendment to claims 13, 14, and 26 to recite “wherein adenosine monophosphate (AMP) is not added to the reaction mixture.” By the amendment to claims 13, 14, and 26 to recite “wherein adenosine monophosphate (AMP) is not added to the reaction mixture,” the instant claims thus exclude commercial sources of pyruvate kinase obtained from rabbit muscle.
Claims 13-17, 21, 25, 26, and 28 are newly rejected on the ground of nonstatutory double patenting as being unpatentable over claims 3-6 of U.S. Patent No. 5,891,659 (patent) in view of Hansen-1, Lumitester PD 10, U.S. Patent No. 5,891,659, Murcott, and Sakai. The instant rejection is necessitated by the amendment to recite “wherein adenosine monophosphate (AMP) is not added to the reaction mixture” in claims 13, 14, and 26.
Claim 3 of the patent recites a method for quantitatively determining an adenosine phosphate ester which comprises reacting a bioluminescence reagent comprising:
(a) pyruvate orthophosphate dikinase,
(b) phosphoenolpyruvic acid,
(c) pyrophosphoric acid,
(d) magnesium ion or another divalent metallic cation,
(e) luciferin and
(f) luciferase
with a sample containing the adenosine phosphate ester, measuring the amount of luminescence formed and then quantitatively determining an amount of the adenosine phosphate ester with a standard curve obtained by using an adenosine phosphate ester standard solution having a predetermined concentration;
Claim 4 of the patent recites the method according to claim 3 which comprises reacting a bioluminescence reagent comprising:
(a) pyruvate orthophosphate dikinase,
(b) phosphoenolpyruvic acid,
(c) pyrophosphoric acid,
(d) magnesium ion or another divalent metallic cation,
(e) luciferin and
(f) luciferase
with a sample containing ATP, and measuring the amount of luminescence formed to determine ATP quantitatively;
Claim 5 of the patent recites the method according to claim 3 which comprises reacting a bioluminescence reagent comprising:
(a) pyruvate orthophosphate dikinase,
(b) phosphoenolpyruvic acid,
(c) pyrophosphoric acid,
(d) magnesium ion or another divalent metallic cation,
(e) luciferin and
(f) luciferase
with a sample containing AMP, and measuring the amount of luminescence formed to determine AMP quantitatively; and
Claim 6 of the patent recites the method according to claim 3 which comprises reacting a bioluminescence reagent comprising:
(a) pyruvate orthophosphate dikinase,
(b) phosphoenolpyruvic acid,
(c) pyrophosphoric acid,
(d) magnesium ion or other divalent metallic cation,
(e) luciferin,
(f) luciferase and
(g) pyruvate kinase
with a sample containing ADP, and measuring the amount of luminescence formed to determine ADP quantitatively.
The claims of the patent do not recite applying the method to the detection of blood or biological contamination on a medical instrument.
Hansen-1 teaches that reprocessing procedures for medical devices is often monitored by determination of residual blood on instruments after reprocessing, however, described methods for detection of blood are too cumbersome to be performed routinely at reprocessing sites for medical devices (p. 1, column 1). Hansen-1 teaches ATP is a constituent of all living cells and teaches ATP bioluminescence assay to verify success of cleaning in reprocessing of medical devices (p. 1, column 2) and for quality control of reprocessing of surgical instruments (p. 3, column 1). More specifically, Hansen-1 discloses using ATP bioluminescence assay to check endoscope reprocessing (p. 2, column 2) and to verify the cleaning of contaminated surgical instruments in the context of validation of washer-disinfectors (p. 3, Figure 4 and column 2). Hansen-1 teaches Lumitester PD 10 for measuring ATP bioluminescence (p. 2, column 2, bottom).
Lumitester PD 10 teaches that because ATP is present in all living cells, it is an indicator of biological contamination (p. 1, middle column). Lumitester PD 10 teaches that the Lumitester takes hygiene monitoring one step further by detecting both ATP and AMP, which improves sensitivity (p. 1, column 1 and middle paragraph). Lumitester PD 10 teaches measuring ATP and AMP bioluminescence by means of an enzyme reaction including pyruvate orthophosphate dikinase, luciferin, luciferase, and Mg2+ (p. 2, bottom). Lumitester PD 10 cites to U.S. Patent No. 5,891,659 (p. 2, bottom).
U.S. Patent No. 5,891,659 teaches that, in addition to measuring AMP bioluminescence (column 8), ADP luminescence can also be measured, wherein ADP is converted to ATP in a reaction comprising pyruvate kinase (columns 9, bottom to column 10, top). According to U.S. Patent No. 5,891,659, the methods of the invention have high sensitivity and high accuracy (column 3, bottom; column 10, bottom).
In view of Hansen, Lumitester PD 10, and U.S. Patent No. 5,891,659, it would have been obvious to one of ordinary skill in the art before the effective filing date to apply the method of the claims of the patent to the detection of blood or biological contamination on a medical instrument. One would have been motivated to and would have had a reasonable expectation of success to do this because Lumitester PD 10 teaches that measuring AMP and ATP bioluminescence has the effect of increasing sensitivity and cites to U.S. Patent No. 5,891,659, and U.S. Patent No. 5,891,659 teaches that, in addition to measuring AMP and ATP bioluminescence, ADP bioluminescence can be measured and discloses that the methods of the invention have high sensitivity and high accuracy.
Regarding the limitation “wherein adenosine monophosphate (AMP) is not added to the reaction mixture” as recited in instant claims 13, 14, and 26, the specification of the patent discloses an exemplary pyruvate kinase made by Boehringer-Mannheim GmbH, which, in view of the evidence of the Second Suzuki Declaration, is obtained from rabbit muscle and contains AMP. However, U.S. Patent No. 5,891,659 teaches acetate kinase or creatine kinase may be used in place of pyruvate kinase (column 10, lines 25-27), and pyruvate kinase obtained from a source other than rabbit muscle was well-known in the prior art before the effective filing date, e.g., Murcott teaches purified pyruvate kinase from yeast (p. 513, abstract) and Sakai teaches purified pyruvate kinase from Bacillus stearothermophilus (p. 1157, abstract).
In view of the teachings of U.S. Patent No. 5,891,659, Murcott, and Sakai, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention for the pyruvate kinase of the claims of the patent to be acetate kinase, creatine kinase, yeast pyruvate kinase, or Bacillus stearothermophilus pyruvate kinase. One would have been motivated and would have expected success for the pyruvate kinase of the claims of the patent to be acetate kinase or creatine kinase because, while the claims of the patent recite a pyruvate kinase, U.S. Patent No. 5,891,659 teaches acetate kinase or creatine kinase may be used in place of pyruvate kinase. One would have been motivated and would have expected success for the pyruvate kinase of the claims of the patent to be yeast pyruvate kinase or Bacillus stearothermophilus pyruvate kinase because neither the claims nor the specification of the patent require a particular pyruvate kinase and Murcott and Sakai each teaches a pyruvate kinase obtained from a source other than rabbit muscle, e.g., Murcott teaches purified pyruvate kinase from yeast and Sakai teaches purified pyruvate kinase from Bacillus stearothermophilus.
Therefore, claims 13-17, 21, 25, 26, and 28 are unpatentable over claims 3-6 of the patent in view of Hansen-1, Lumitester PD 10, U.S. Patent No. 5,891,659, Murcott, and Sakai.
RESPONSE TO REMARKS: Applicant argues that given the numerous differences in techniques, procedures and protocols of the claims of the patent and the cited references of Hansen, Lumitester PD 10, and U.S. Patent No. 5,891,659, it would not have been obvious to arrive at the invention of the claims of this application.
Applicant’s argument is not found persuasive. At least for the reasons set forth above, claims 13-17, 21, 25, 26, and 28 are unpatentable over claims 3-6 of the patent in view of Hansen-1, Lumitester PD 10, U.S. Patent No. 5,891,659, Murcott, and Sakai.
Claims 13-17, 21, 25, 26, and 28 are newly provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 15 of co-pending application 17/799,134 (reference application) in view of Champiat, D. (US 2008/0014607 A1; cited on Form PTO-892 mailed September 21, 2021; hereafter “Champiat”), Hansen-1, Murcott, and Sakai. The instant provisional rejection is necessitated by the amendment to recite “wherein adenosine monophosphate (AMP) is not added to the reaction mixture” in claims 13, 14, and 26.
Claim 15 is drawn to a method for measuring ATP and AMP and/or ADP in a sample, comprising bringing the liquid composition according to claim 1 into contact with a sample and measuring the level of luminescence.
The differences between the claim of the reference application and the claims of this application are:
1) the claim of the reference application does not recite an enzyme that catalyzes a reaction that produces ATP from ADP and a metal salt; and
2) the claim of the reference application does not recite applying the method to the detection of blood or biological contamination on a non-blood derived sample or medical instrument by ATP bioluminescence assay.
Regarding difference 1), the reference of Champiat teaches an ATP bioluminescence assay by determining the adenyl nucleotides (ATP, ADP, and AMP) in a sample (paragraph [0046]). Champiat’s method comprises using pyruvate kinase, luciferin, luciferase, and pyruvate orthophosphate dikinase in a Tris buffer (Example 2, paragraphs [0073] and [0074]). Champiat teaches the luciferase reaction requires Mg2+ (paragraph [0013]) and teaches Tris buffer with magnesium salt (paragraph [0127]).
In view of the teachings of Champiat, it would have been obvious to one of ordinary skill in the art to modify the method of claim 15 of the reference application to include a magnesium salt and pyruvate kinase. One would have been motivated to and would have expected success to include a magnesium salt because the method of the claim of the reference application includes a luciferase reaction and Champiat teaches the luciferase reaction requires Mg2+. One would have been motivated to and would have expected success to include pyruvate kinase because the method of the claim of the reference application detects ATP, ADP, and AMP and Champiat teaches a method for detecting ATP, ADP, and AMP in a luciferase reaction including pyruvate kinase.
Regarding difference 2), the reference of Hansen-1 teaches that reprocessing procedures for medical devices is often monitored by determination of residual blood on instruments after reprocessing, however, described methods for detection of blood are too cumbersome to be performed routinely at reprocessing sites for medical devices (p. 1, column 1). Hansen-1 teaches ATP is a constituent of all living cells and teaches ATP bioluminescence assay to verify success of cleaning in reprocessing of medical devices (p. 1, column 2) and for quality control of reprocessing of surgical instruments (p. 3, column 1). More specifically, Hansen-1 teaches using ATP bioluminescence assay to check endoscope reprocessing (p. 2, column 2) and to verify the cleaning of contaminated surgical instruments in the context of validation of washer-disinfectors (p. 3, Figure 4 and column 2).
In view of the teachings of Hansen-1, it would have been obvious to one of ordinary skill in the art to apply the method of claim 15 for detecting blood or biological contamination. One would have been motivated to and would have had a reasonable expectation of success to apply the method of claim 15 for detecting blood or biological contamination because Hansen-1 teaches ATP bioluminescence assay for blood contamination on surgical instruments.
Regarding the limitation “wherein adenosine monophosphate (AMP) is not added to the reaction mixture” as recited in instant claims 13, 14, and 26, Champiat does not specify the source of the pyruvate kinase. However, even if the pyruvate kinase of Champiat is obtained from rabbit muscle and comprises AMP, pyruvate kinase obtained from a source other than rabbit muscle was well-known in the prior art before the effective filing date, e.g., Murcott teaches purified pyruvate kinase from yeast (p. 513, abstract) and Sakai teaches purified pyruvate kinase from Bacillus stearothermophilus (p. 1157, abstract).
In view of the teachings of Murcott and Sakai, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention for the pyruvate kinase taught by Champiat to be yeast pyruvate kinase or Bacillus stearothermophilus pyruvate kinase. One would have been motivated and would have expected success for the pyruvate kinase taught by Champiat to be yeast pyruvate kinase or Bacillus stearothermophilus pyruvate kinase because Champiat does not teach a particular pyruvate kinase and Murcott and Sakai each teaches a pyruvate kinase.
Therefore, claims 13-17, 21, 25, 26, and 28 of this application are unpatentable over claim 15 of the reference application in view of Champiat, Hansen-1, Murcott, and Sakai. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
RESPONSE TO REMARKS: Applicant argues that given the numerous differences in techniques, procedures and protocols of the claims of the reference application and the cited references of Champiat and Hansen-1, it would not have been obvious to arrive at the invention of the claims of this application.
Applicant’s argument is not found persuasive. At least for the reasons set forth above, claims 13-17, 21, 25, 26, and 28 of this application are unpatentable over claim 15 of the reference application in view of Champiat, Hansen-1, Murcott, and Sakai.
Claims 13-17, 21, 25, 26, and 28 are newly provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4, and 7 of co-pending application 18/997,307 (reference application) in view of Champiat, Hansen-1, Murcott, and Sakai. The instant provisional rejection is necessitated by the amendment to recite “wherein adenosine monophosphate (AMP) is not added to the reaction mixture” in claims 13, 14, and 26.
Claim 1 of the reference application recites a method for detecting a microorganism or cell, comprising the steps of:
(i) extracting an adenine nucleotide component of the microorganism or cell by bringing an extracting agent containing a surfactant into contact with a solution that may contain the microorganism or cell without allowing any surfactant adsorbent to be in contact with the solution that may contain the microorganism or cell,
(ii) bringing an analyte comprising the adenine nucleotide component derived from the microorganism or cell, resulting from the extraction of step (i), into contact with a surfactant adsorbent;
(iii) bringing the sample contacted with the surfactant adsorbent into contact with a luminescence reagent comprising luciferase and luciferin, or suspending the sample contacted with the surfactant adsorbent in a solution and then bringing the solution suspending the sample into contact with a luminescence reagent comprising luciferase and luciferin; and
(iv) measuring luminescence level;
claim 4 of the reference application recites the method according to claim 3, wherein the method is a method for detecting a microorganism or cell, the extracting agent is an extracting agent for a microorganism or an extracting agent for a cell for extracting ATP from the microorganism or cell, the adenine nucleotide is ATP, and step (iii) includes allowing ATP to cause luminescence by luciferase; and
claim 7 recites the method according to claim 4, wherein the luminescence reagent further comprises an enzyme that produces ATP from AMP, and an enzyme that produces ATP from ADP.
The differences between the claims of the reference application and the claims of this application are:
1) the claims of the reference application do not recite a metal salt and do not specify the enzymes; and
2) the claims of the reference application do not recite applying the method to the detection of blood or biological contamination on a non-blood derived sample or medical instrument.
Regarding difference 1), the reference of Champiat teaches an ATP bioluminescence assay by determining the adenyl nucleotides (ATP, ADP, and AMP) in a sample (paragraph [0046]). Champiat’s method comprises using pyruvate kinase, luciferin, luciferase, and pyruvate orthophosphate dikinase in a Tris buffer (Example 2, paragraphs [0073] and [0074]). Champiat teaches the luciferase reaction requires Mg2+ (paragraph [0013]) and teaches Tris buffer with magnesium salt (paragraph [0127]).
In view of the teachings of Champiat, it would have been obvious to one of ordinary skill in the art to modify the method of the claims of the reference application to include a magnesium salt and pyruvate kinase as the enzyme that produces ATP from ADP. One would have been motivated to and would have expected success to include a magnesium salt because the method of the claim of the reference application includes a luciferase reaction and Champiat teaches the luciferase reaction requires Mg2+. One would have been motivated to and would have expected success to include pyruvate kinase because the method of the claims of the reference recite an enzyme that produces ATP from ADP and Champiat teaches pyruvate kinase produces ATP from ADP.
Regarding difference 2), the reference of Hansen-1 teaches that reprocessing procedures for medical devices is often monitored by determination of residual blood on instruments after reprocessing, however, described methods for detection of blood are too cumbersome to be performed routinely at reprocessing sites for medical devices (p. 1, column 1). Hansen-1 teaches ATP is a constituent of all living cells and teaches ATP bioluminescence assay to verify success of cleaning in reprocessing of medical devices (p. 1, column 2) and for quality control of reprocessing of surgical instruments (p. 3, column 1). More specifically, Hansen-1 teaches using ATP bioluminescence assay to check endoscope reprocessing (p. 2, column 2) and to verify the cleaning of contaminated surgical instruments in the context of validation of washer-disinfectors (p. 3, Figure 4 and column 2).
In view of the teachings of Hansen-1, it would have been obvious to one of ordinary skill in the art to apply the method of the claims of the reference application for detecting blood or biological contamination. One would have been motivated to and would have had a reasonable expectation of success to apply the method of the claims of the reference application for detecting blood or biological contamination because Hansen-1 teaches ATP bioluminescence assay for blood contamination on surgical instruments.
Regarding the limitation “wherein adenosine monophosphate (AMP) is not added to the reaction mixture” as recited in instant claims 13, 14, and 26, Champiat does not specify the source of the pyruvate kinase. However, even if the pyruvate kinase of Champiat is obtained from rabbit muscle and comprises AMP, pyruvate kinase obtained from a source other than rabbit muscle was well-known in the prior art before the effective filing date, e.g., Murcott teaches purified pyruvate kinase from yeast (p. 513, abstract) and Sakai teaches purified pyruvate kinase from Bacillus stearothermophilus (p. 1157, abstract).
In view of the teachings of Murcott and Sakai, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention for the pyruvate kinase taught by Champiat to be yeast pyruvate kinase or Bacillus stearothermophilus pyruvate kinase. One would have been motivated and would have expected success for the pyruvate kinase taught by Champiat to be yeast pyruvate kinase or Bacillus stearothermophilus pyruvate kinase because Champiat does not teach a particular pyruvate kinase and Murcott and Sakai each teaches a pyruvate kinase.
Therefore, claims 13-17, 21, 25, 26, and 28 of this application are unpatentable over claims 1, 4, and 7 of the reference application in view of Champiat, Hansen-1, Murcott, and Sakai. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
RESPONSE TO REMARKS: Applicant argues that given the numerous differences in techniques, procedures and protocols of the claims of the reference application and the cited references of Champiat and Hansen-1, it would not have been obvious to arrive at the invention of the claims of this application.
Applicant’s argument is not found persuasive. At least for the reasons set forth above, claims 13-17, 21, 25, 26, and 28 of this application are unpatentable over claims 1, 4, and 7 of the reference application in view of Champiat, Hansen-1, Murcott, and Sakai.
Conclusion
Status of the claims:
Claims 1-5, 9, 10, 13-17, 21, 25, 26 and 28 are pending.
Claims 1-5, 9, and 10 are withdrawn.
Claims 13-17, 21, 25, 26, and 28 are rejected.
No claim is in condition for allowance.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/David Steadman/Primary Examiner, Art Unit 1656