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 .
Claims Status
Claims 1-18 are pending.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 02/13/2025, 04/15/2025, 10/01/2025, or 09/25/2026 is acknowledged. The submission is in compliance with the provision of 37 CFR 1.97. Accordingly, the information disclosure statements have been considered.
Claim Objections
Claim 1 is objected to because of the following informalities: Claim 1 recites “wherein the second composition and the third composition are independently fixed in solid state to the reagent fixing part in respectively. The recitation of “in respectively” is odd or a grammatical error. Appropriate correction is required.
Claim 1 is objected to because of the following informalities: Claim 1 recites “analysis of 1,5-AG”. It is suggested that since the abbreviation 1,5-AG is used for the first time in claim 1, it should be written out completely followed by the abbreviation in parenthesis. Appropriate correction is required.
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.
Claims 1-18 are 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.
With regards to claim 1 (claims 2-18 dependent on) the claim recites “comprises at least one reagent fixing part”. It is unclear what comprises a “fixing part”. The specification does not define what constitutes a “reagent fixing part”. In the interest of advancing prosecution, the Examiner is interpreting a “reagent fixing part” as any surface to which components of the reaction are tethered”
With regards to claims 12-15, it is unclear how claims 12-15 further limit claim 1 from which they depend given the statement in each “whereby fixing…:”. Are these methods? Limitations of the kit?
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 and 5-8 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (CN111575339A; published August 25, 2020), hereinafter referred to as Wang, in view of Dong-heon et al. (KR101974515B1; published May 7, 2019), hereinafter referred to as Dong-heon.
With regards to claim 1, Wang discloses a 1,5-anhydroglucitol quantification kit (see claim 4).
Wang discloses that the kit contains glucose dehydrogenase (first composition, glucose removal), an enzyme system comprising adenosine triphosphate-dependent hexokinase, oxidized coenzyme II and 1,5-anhdyroglucitol dehydrogenase which is used to react with 1,5-anhydroglucitol (second composition, glucitol reaction reagent), a stabilizer (see paragraph 0060) and a chromogenic agent, DA-67, (third composition) (see paragraph 0060 and 0047). Wang further discloses that the reagents of the present invention maybe prepared as a lyophilized product (solid state) (see paragraph 0067).
Wang does not teach that the kit comprises at least one reagent fixing part wherein the second composition and the third composition are independently fixed in solid state to the reagent fixing part.
However, Dong-heon teaches a kit for quantitative analysis of glycated hemoglobin which may comprise a plurality of reagent fixing parts, wherein the first composition, second composition, and third composition are independently fixed to the plurality of reagent fixing parts. Dong-heon further teaches that the compositions are preferably fixed to the reagent fixing part portion in a dry state (solid) (see paragraph 0068). Dong-heon teaches that a reagent fixing part in which a sample is fixed so as to react with the mixture (see paragraph 0078).
It would have been obvious to one of ordinary skill in the art of analytical biochemistry before the effective filing date of the current instant application to modify the kit taught by Wang by independently fixing the second composition and third composition in solid state to the reagent fixing part as taught by Dong-heon. One of ordinary skill in the art would find the motivation to do so in the teachings of Dong-heon who teaches that compositions are independently fixed to reagent fixing parts and preferably in a dry state which provides a means of tethering the composition to the surface so that the sample is fixed and allow the enzymes to react with the mixed solution in the kit. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Wang and Dong-heon who provide all the necessary teachings and methods to do so.
With regards to claims 5-8, neither Wang nor Dong-heon specifically teach the kit contains a glucose-scavenging enzyme that is a glucose converting enzyme for generating a product including glucose-6-phosphate from a reactant including the glucose in the sample where the glucose converting-enzyme is selected from the group consisting of glucokinase (GK), hexokinase, and mixtures thereof; or a reverse reaction removal agent for inhibiting reverse reaction from the glucose-6-phospahte back to glucose where the reverse reaction removal reagent comprises pyruvate kinase and phosphoenolpyruvic acid (PEP), and the further comprises ATP.
However, Wang does teach that it is known that commercial kits for quantifying 1,5-anhydroglucitol all have to eliminate interference of glucose in the sample (see paragraph 0005). Wang teaches that the kit contains a glucose-scavenging enzyme system comprising coenzyme I, glucose dehydrogenase, and NAD-dependent malate dehydrogenase to scavenge interference caused by cross reaction of glucose in the sample (see Abstract and paragraph 0008). Wang further teaches that current enzymatic methods for measuring 1,5-anhydrogluctiol mainly include the pyranose oxidase method which uses glucose kinase and pyruvate kinase to remove the interference of glucose from the sample (see paragraph 0006).
It would have been obvious to one of ordinary skill in the art of protein biochemistry before the effective filing date of the current instant application to modify the 1,5-anhydroglucitol quantification kit arrived at from the teachings of Wang and Dong-heon by substituting the glucose-scavenging enzyme system with glucose kinase and pyruvate kinase since Wang also teaches that these enzymes are known in the art to function to eliminate interference of glucose in the sample (see paragraph 0006). Furthermore, it would have been obvious to one of ordinary skill in the art to include phosphoenolpyruvic acid (PEP) and ATP in the kit since PEP is a substrate of pyruvate kinase as evidenced by Gupta et al. (Protein Science, Vol. 19, pg. 2031-2044; published November 2010) who teaches that pyruvate kinases catalyzes the transphosphorylation from PEP to ADP (see pg. 2031) and Zhang et al. (PlosOne, Vol. 4(7):e6304; published July 20, 2009) who teaches that ATP is a substrate of glucokinase (see Abstract), respectivley. One of ordinary skill in the art would be motivated to do so since Wang teaches that this is an alternative way of scavenging glucose from the sample to avoid interference from glucose in the quantification of 1,5-anhydroglucitol. One of ordinary skill in the art would have expectations in doing so since the combined teachings of Wang and Dong-heon provide all the teachings and methods needed to do so.
Therefore, claims 1 and 5-8 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (CN111575339A; published August 25, 2020), hereinafter referred to as Wang, in view of Dong-heon et al. (KR101974515B1; published May 7, 2019).
Claims 2-4 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (CN111575339A; published August 25, 2020), hereinafter referred to as Wang, in view of Dong-heon et al. (KR101974515B1; published May 7, 2019), hereinafter referred to as Dong-heon, as applied to claim 1 above, and further in view of Lee et al. (Journal of Biological Chemistry, Vol. 256, pg. 7193-7201; published 1981), hereinafter referred to as Lee.
The teachings of Wang and Dong-heon as applied to claim 1 are summarized above.
With regards to claims 2-4, Neither Wang nor Dong-heon specifically teach that the stabilizer in the 1,5-anhydroglucitol quantification kit is selected from the group consisting of sucrose, trehalose, lactose, maltose, turanose, cellobiose, dextran, diethylamino ethyldextran, dextrin, cellulose, and beta-glucans.
However, Lee teaches that sucrose provides protein stabilization (see Abstract, pg. 7193). Lee further teaches observations testing the effect of sucrose concentration on protein stabilization in the range of 0-1 M concentration. (See Table 1, pg. 7194).
It would have been obvious to one of ordinary skill in the art of protein biochemistry before the effective filing date of the current instant application to use sucrose as stabilizer in the 1,5-anhydroglucitol quantification kit taught by Wang and Dong-heon. It would have also been obvious to one of ordinary skill in the art to arrive at a concentration range of 160-200 mM or 90 mM-360 mM for the sucrose concentration in the second composition of the kit based on the suggested value range taught by Lee (see Table 1, pg. 7194). It is well settled that “discovery of an optimum value of a result effective variable in a known process is ordinarily within the skill of the art. In re Boesch, 617 F.2d 272, 276, 205 USPQ 215, 219 (CCPA 1980) and where the general conditions of a claim are disclosed in the prior art, discovering the optimum or workable ranges involves only routine skill in the art. In re Aller, 220 F2d 454, 456, 105 USPQ 233; 235 (CCPA 1955). One of ordinary skill in the art would be motivated to do so by the combined teachings of Wang, Dong-heon and Lee in order to provide a reagent that will stabilize the enzymes/proteins in the kit during reaction in solution. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Wang, Dong-heon, and Lee who provide all the teachings and methods needed to do so.
Therefore, claims 2-4 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (CN111575339A; published August 25, 2020) in view of Dong-heon et al. (KR101974515B1; published May 7, 2019), as applied to claim 1 above, and further in view of Lee et al. (Journal of Biological Chemistry, Vol. 256, pg. 7193-7201; published 1981).
Claims 9-11 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (CN111575339A; published August 25, 2020), hereinafter referred to as Wang, in view of Dong-heon et al. (KR101974515B1; published May 7, 2019), hereinafter referred to as Dong-heon, as applied to claim 1 above, and further in view of Machida et al. (US Patent No.: US 8,883,439 B2; published November 11, 2014), hereinafter referred to as Machida.
The teachings of Wang and Dong-heon as applied to claim 1 are summarized above.
Neither Wang nor Dong-heon specifically teach that the kit comprises a first-reaction enzyme generating hydrogen peroxide by reacting with the 1,5-AG in the sample and a second reaction enzyme oxidizing the chromogenic agent by reacting with the hydrogen peroxide.
However, Machida teaches a method for measuring a concentration of analyte using whole blood and where the analyte generates hydrogen peroxide when an oxidase is reacted with it (see lines 47-54, column 2). Machida teaches that the analyte is 1,5-anhydroglucitol and that the oxidase is pyranose oxidase (see column 3, section 9-10). Machida teaches that the reagents for detecting the hydrogen peroxide are peroxidase and a chromogen, DA67 (see column 3, section 13 and column 6, lines 32-36).
It would have been obvious to one of ordinary skill in the art of analytical biochemistry before the effective filing date of the current instant application to modify the kit taught by Wang and Dong-heon by incorporating pyranose oxidase as the first reacting enzyme that reacts with 1,5-AG to form hydrogen peroxide and incorporating peroxidase as the second enzyme that reacts with the hydrogen peroxide to oxidize the chromogenic agent. One of ordinary skill in the art would find motivation to do so from the teachings of Manchida who demonstrates that reaction of pyranose oxidase with 1,5-AG results in the formation of hydrogen peroxide which can then be detected by reaction with peroxidase which in turn would oxidize the chromogenic agent and give a signal that can be detected and correlated to the analyte. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Wang, Dong-heon, and Machida who provide all the teachings, compositions, and methods needed to do so.
Therefore, claims 9-11 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (CN111575339A; published August 25, 2020) in view of Dong-heon et al. (KR101974515B1; published May 7, 2019) as applied to claim 1 above, and further in view of Machida et al. (US Patent No.: US 8,883,439 B2; published November 11, 2014).
Claims 12-15 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (CN111575339A; published August 25, 2020), hereinafter referred to as Wang, in view of Dong-heon et al. (KR101974515B1; published May 7, 2019), hereinafter referred to as Dong-heon as applied to claim 1 above, and further in view of Minteer et al. (US Patent Application No. US 2010/0041123 A1; published Feb. 18, 2010), hereinafter referred to as Minteer.
With regards to claims 12-15, neither Wang or Dong-heon teach that by fixing and storing the second composition in solid state to the fixing part, the activity of the glucitol reagent is maintained at 66%, 85% or more of its initial activity even after 38 or 326 days.
However, Minteer teaches the immobilization an enzyme for use in an application wherein enzyme stability is advantageous (see paragraph 030). Minster teaches that in the invention, an enzyme is stabilized if it retains at least about 75% of its initial catalytic activity for at least 30 days to about 365 days (see paragraph 030). Minteer teaches that the enzyme is immobilized in an enzyme immobilization material (see paragraph 0036) Minteer teaches a variety of immobilization agents that can be used such as hydrophobic cations (see paragraph 0049) and modified perfluoro sulfonic acid-PTFE copolymer (see paragraph 0044).
It would have been obvious to one of ordinary skill in the art of enzyme assays before the effective filing date of the current instant application to modify the teachings of Wang and Dong-heon by testing different immobilization agents as taught by Minteer in order to stabilize the enzyme reagents in the kit for detecting 1.5-anhydroglucitol by immobilization. One of ordinary skill in the art would be motivated to do so by the teachings of Minteer who teaches that immobilization of enzymes allows the enzymes to retain initial catalytic activity for an extended amount of time. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Wang, Dong-heon, and Minteer who provide all the necessary teachings, components, and methods needed to do so.
Therefore, claims 12-15 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (CN111575339A; published August 25, 2020), in view of Dong-heon et al. (KR101974515B1; published May 7, 2019) as applied to claim 1 above, and further in view of Minteer et al. (US Patent Application No. US 2010/0041123 A1; published Feb. 18, 2010).
Claims 16-18 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (CN111575339A; published August 25, 2020), hereinafter referred to as Wang, in view of Dong-heon et al. (KR101974515B1; published May 7, 2019), hereinafter referred to as Dong-heon as applied to claim 1 above, and further in view of Park et al. (US Patent Application Publication No. US 2015/0160206 A1; published June 11, 2015), hereinafter referred to as Park.
The teachings of Wang and Dong-heon as applied to claim 1 are summarized above.
With regards to claim 16, neither Wang or Dong-heon teach that the kit comprises a body including an upper plate and a lower plate configured to face each other, wherein the second composition is fixed to a first reagent fixing part located in a first compartmental region of the lower plate, and wherein the third composition is fixed to a first reagent fixing part located in the first compartmental region of the lower plate, and wherein the first reagent fixing part and the second reagent fixing part are configured to face each other.
With regards to claim 17, neither Wang nor Dong-heon teach that the kit comprises a solution cell disposed in a second compartmental region portioned from the first compartmental region.
With regards to claim 18, neither Wang nor Dong-heon teach that the kit comprises a flow path into a mixing region within the second compartmental region.
However, Park teaches a microfluidic device that is capable of rapidly performing an in vitro diagnosis which includes a platform which includes a sample injection whole through which a sample may be injected and a chamber which is formed in the platform in which a first reagent and a second reagent are stored. (see abstract). Park teaches that the platform may include a film-shaped upper plate and a film-shaped lower plate and the chamber may be formed by bonding the upper plate with the lower plate (see paragraph 0014). Park also teaches that the microfluidic device may further include a channel that is formed at the platform and which is configured to connect the sample injection hole with the chamber (see paragraph 0016). Park teaches that the microfluidic device may further include a sample accommodation chamber that is formed at the platform and which is configured to accommodate the sample injected through the sample injection hole (see paragraph 0018). Park teaches that a first reagent may be applied to the first position of the inner walls of the chamber and then dried and the second reagent may be applied at a second position of the inner walls of the chamber and then may be dried wherein the second position is different from the first (see paragraph 0020). Park teaches that the microfluidic device may further include a channel configured to connect the chamber with the sample accommodation chamber. Park teaches that the chamber is formed in the platform which is configured to store a first reagent which includes first enzymes that primarily decompose hemoglobin that exists in the sample and a second reagent which includes second enzymes that secondarily decompose the decomposed hemoglobin (see paragraph 0025). Park teaches that the microfluidic device may further include a sample accommodation chamber that is formed at the platform which is configured to accommodate the sample injected through the sample injection hole, wherein the platform may be rotatable and the sample accommodation chamber may be disposed closer to the center of ration of the platform than the chamber (see paragraph 0029). Park teaches that the microfluidic device may move materials within the microfluidic device by using a centrifugal force caused by rotation (see paragraph 0139).
It would have been obvious one of ordinary skill in the art of enzyme assays and diagnostics to modify the kit for detecting 1,5-anhydroglucitol taught by Wang and Dong-heon by including a microfluidic device as taught by Park in order to allow for mixing of reagents to allow for the reactions to occur for detecting 1,5-anhydroglucitol. It would have been obvious to place the first and second reagent fixing part taught by Wang and Dong-heon in place of the first reagent and second reagent in the upper and lower film plates taught by Park and to use the sample injection port for introduction of the analyte taught by Wang. One of ordinary skill in the art would find it obvious to place the second composition comprising a glucitol reaction reagent and the third composition comprising the chromogenic agent taught by Wang in place in the upper and lower plates and the first composition comprising the glucose removal reagent taught by Wang in the sample cell taught by Park. One would find this set up obvious as the sample of interest would first encounter the solution cell containing the glucose removal reagent followed by passage into the compartment containing the glucitol reagent and the chromogen agent to allow for the reaction to occur after removal of glucose occurs in the sample cell by the glucose removal reagent thus removing potential interference from the presence of glucose in the detection of 1,5-anhydroglucitol. One of ordinary skill in the art would find motivation to do so from the teachings of Park who describes a microfluid diagnostic device that is configured to run a diagnostic assay which incudes a sample compartment and a second compartment having multiple enzyme reagents. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Wang, Dong-heon, and Park who provide all the necessary teachings, components, and methods needed to do so.
Therefore, claims 16-18 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (CN111575339A; published August 25, 2020), in view of Dong-heon et al. (KR101974515B1; published May 7, 2019) as applied to claim 1 above, and further in view of Park et al. (US Patent Application Publication No. US 2015/0160206 A1; published June 11, 2015).
Conclusion
No claims are allowed.
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/GEORGE THEMISTOCLIS LOUNTOS/ Examiner, Art Unit 1652
/ROBERT B MONDESI/ Supervisory Patent Examiner, Art Unit 1652
