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 .
In view of the appeal brief filed on 6/22/2026, PROSECUTION IS HEREBY REOPENED. New grounds of rejection are set forth below.
To avoid abandonment of the application, appellant must exercise one of the following two options:
(1) file a reply under 37 CFR 1.111 (if this Office action is non-final) or a reply under 37 CFR 1.113 (if this Office action is final); or,
(2) initiate a new appeal by filing a notice of appeal under 37 CFR 41.31 followed by an appeal brief under 37 CFR 41.37. The previously paid notice of appeal fee and appeal brief fee can be applied to the new appeal. If, however, the appeal fees set forth in 37 CFR 41.20 have been increased since they were previously paid, then appellant must pay the difference between the increased fees and the amount previously paid.
A Supervisory Patent Examiner (SPE) has approved of reopening prosecution by signing below:
/MANJUNATH N RAO/Supervisory Patent Examiner, Art Unit 1656
Claims 42, 44-47, 49-50, 54-59, 61-64 are pending.
Claims 62-64 stand withdrawn from consideration pursuant to 37 CFR 1.142(b).
Claims 1-41, 43, 48, 51-53, 60 , 65-67 are cancelled.
Claims 42, 44-47, 49-50, 54-59, 61 are pending and examined on the merits.
Appellant’s Appeal Brief filed on 6/22/2026 in response to the Final Rejection mailed on 12/22/2025 have been fully considered and are not deemed persuasive to overcome at least one of the rejections and/or objections as previously applied.
The text of those sections of Title 35 U.S. Code not included in the instant action can be found in the prior Office Action.
New 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 49-50 are newly 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 respect to claim 49, claim 42 states that “the system” further comprises ferrocyanide. Claim 49 states that “wherein the first or the second reagent” contains the ferrocyanide. However, it is both the first and the second reagent that form the “system” which comprises the ferrocyanide. Therefore, claim 49 is not further limiting claim 42. Appropriate correction is suggested.
With respect to claim 50, claim 42 states that “the second reagent contains a combination of a protease and a stabilizer of the protease” and further comprises ferrocyanide. Claim 50 recites “wherein the second reagent contains the protease, the stabilizer of the protease, and the ferrocyanide.” However, it is the second reagent that contains the protease, the stabilizer of the protease, and the ferrocyanide, as recited in claim 42. Therefore, claim 50 is not further limiting claim 42. Appropriate correction is suggested.
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 text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
The rejection of claims 42, 44-47, 49-50, 56, 58-59, 61 under 35 U.S.C. 103 as being unpatentable over Torrens et al (US Patent No: 6,008,006, Date of Patent: Dec. 28, 1999, cited on PTO-892 dated 1/24/2025) {herein Torrens} in view of Kouzuma et al (US Patent Application No: US 2005/0101771 A1, Date of Publication: May 12, 2005, cited on IDS filed on 2/11/2022) {herein Kouzuma} is maintained. The rejection has been modified in view of Applicant’s Appeal Brief dated 6/22/2026.
Claims 42, 44-47, 49-50, 56, 58-59, 61 are drawn to a glycated protein assay reagent system containing a first reagent and a second reagent, wherein the first reagent contains a Trinder reagent, the second reagent contains 4-aminoantipyrine, the first reagent or the second reagent contains a combination of a protease and a stabilizer of the protease, the stabilizer of the protease is at least one member selected from the group consisting of propylene glycol, trimethylene glycol, ethylene glycol and carboxyphenylboronic acid, the reagent system further contains a ferrocyanide.
With respect to claims 42, 44-47, 49, 50, 61, Torrens teaches glycated protein assay reagents containing: a trinder (peroxidase), aminoantipyrene, protease (proteinase K) and ferrocyanide (column 9, lines 14-26). The first reagent contains peroxidase (a trinder) (column 6, line 52) and proteinase K, (column 9, lines 11-12, 21-25). The second reagent contains 4-aminoantipyrine (column 6, lines 53-54). Torrens further teaches the protein assays may also contain fructosyl amino acid oxidase (column 2, lines 47-48) , thereby meeting the limitation of claim 45 of ‘the second reagent further contains fructosyl amino acid oxidase.’
With respect to claim 58, Torrens teaches in the blood, the main proteins that are glycated is albumin (column 1, lines 57-58).
With respect to claim 59, Torrens teaches the glycated protein reagent is stored at 4C (column 6, lines 17-18). Examiner is interpreting the teaching of ‘stored’ by Torrens to be the same as ‘preserved’ within the instant application as both processes involve the glycated protein being held at a temperature for a period of time.
However, Torrens does not teach at least one member selected from the group consisting of propylene glycol, trimethylene glycol, ethylene glycol and carboxyphenylboronic acid (claim 42) to be used as a stabilizer of the protease. Or, the product of claim 44, wherein the first reagent contains the combination of the protease and the stabilizer of the protease (claim 44). Or, the product of claim 56, wherein, the stabilizer of the protease is ethylene glycol, and the concentration of the ethylene glycol in the first reagent or the second reagent is from 40 wt/vol% to 80wt/vol% (claim 56).
With respect to claims 42, 44, 56 Kouzuma teaches a glycated protein assay with ethylene glycol as a protease stabilizer (para 0155 and para 0309). Kouzuma surprisingly found that the stabilizer exhibited a high stabilization effect to a degree that almost no decrease in the activity is seen when stored in a liquid state for four days (para 0029).
Although the references of Torrens in view of Kouzuma do not explicitly teach the limitations of claim 56 regarding the concentration of the ethylene glycol in the 4- aminoantipyrine-containing partial composition or the Trinder reagent-containing partial composition from 40 wt/vol% to 80 wt/vol%, MPEP 2144.05 states"[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (MPEP 2144.05 IIA)." One of ordinary skill would desire to optimize the concentration of the ethylene glycol depending on the particular application. It would be routine for one to arrive at the concentration of ethylene glycol for the application they intend on using the glycated protein assay. Therefore, the above invention would have been prima facie obvious
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to apply the teachings of Torrens et al of a glycated protein assay reagent or combine the teachings of Kouzuma because Kouzuma teaches a glycated protein assay where ethylene glycol is a protease stabilizer (para 0155). Whereas Torrens teaches a glycated protein assay reagent containing: a trinder (peroxidase), aminoantipyrene, protease (proteinase K), a stabilizer of the protease (mannitol) and ferrocyanide (column 9, lines 14-26).
One of ordinary skill in the art would be motivated to either use the teachings of Torrens et al. by itself of combine the teachings of Torrens and Kouzuma because Kouzuma teaches ethylene glycol is a protease stabilizer that can suppress a decrease in protease activity during storage of the reagent within assays containing glycated proteins (para 0154), even in a liquid state (para 0154). As such, one of ordinary skill in the art would be motivated to combine the teachings of Torrens and Kouzuma as doing so would result in a composition comprising protease that maintains and extends the activity of the reagent within glycated assays and its shelf-life during storage. One of ordinary skill in the art knowing the benefit of maintaining protease activity within a glycated protein assay based on the teachings of Torrens and Kouzuma would have a reasonable expectation of success to substitute the glycated assay reagents taught by Torrens with the protease stabilizer taught by Kouzuma (ethylene glycol) because Kouzuma teaches ethylene glycol can suppress a decrease in protease activity within glycated protein assays during storage, even in a liquid state (para 0154). MPEP 2143.I.B states “the rationale to support a conclusion that the claim would have been obvious is that the substitution of one known element for another yields predictable results to one of ordinary skill in the art.” Thereby, utilizing ethylene glycol as a protease stabilizer would result in a glycated protein assay with extended protease activity even after storage. Additionally, the utilization of the ethylene glycol as the protease stabilizer would reduce the likelihood of the glycated protease assay from losing its full activity over a period of time, thereby resulting in reduced costs that would be associated with having to purchase additional reagents.
One of skill in the art would have a reasonable expectation of success to make and use the claimed protease stabilizer because Kouzuma provides the teaching of ethylene glycol as a protease stabilizer (para 0155 and para 0309) that can suppress a decrease in the protease activity during storage of the reagent in a liquid state (para 0154). Whereas Torrens provides the teaching of glycated protein assay reagents containing: a trinder (peroxidase), aminoantipyrene, protease (proteinase K) and ferrocyanide (column 9, lines 14-26). Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
RESPONSE TO REMARKS: Applicant’s appeal filed 6/22/2026 have been fully considered but they are not persuasive in view of the rejection set forth. Beginning on p. 4 of Applicant’s remarks, Applicant in summary submits that the Examiner has not established a proper prima facie case of obviousness because (a) there is no motivation to combine the references in the manner suggested by the Examiner and (b) the references do not teach all of the limitations of the claims even if the references are combined.
Examiner contends that the arguments with respect to each grouping of the claims on appeal, the Torrens reference, the Declaration of Mr. Shota KONNO (Exhibit 1), test results reported in the Declaration submitted under Rule 132, have been considered. In view of Applicant’s remarks dated 6/22/2026, Examiner is now presenting a new 103 rejection although it is based on the same references as the final dated 12/22/2025. Examiner contends that one of ordinary skill in the art would be motivated to combine the teachings of Torrens and Kouzuma because Kouzuma teaches ethylene glycol is a protease stabilizer that can suppress a decrease in protease activity during storage of the reagent (para 0154), even in a liquid state (para 0154), thereby utilizing said stabilizer would extend and maintain the activity of the reagent and its shelf-life during storage. Additionally, the utilization of the ethylene glycol as the protease stabilizer would reduce the likelihood of the glycated protease assay from losing its activity, thereby resulting in reduced costs that would be associated with having to purchase additional reagents. Examiner acknowledges Applicant’s assertion that the tests reported by Applicant in the Konno Declaration show that the protease stabilizers recited in claim 42 exhibited unexpectedly improved results over DMSO. Furthermore, Examiner acknowledges Applicant’s Declaration that the stabilizers of the present invention provide unexpectedly improved results as compared to the stabilizers described in the prior art. However, Examiner reminds Appellant that the degree upon which the stabilizer ‘improves’ the protease activity during storage within the glycated protein assay is not what is being claimed. Examiner contends that Applicant is claiming a glycated protein assay reagent with a protease and a variety of protease stabilizers in various concentrations. Examiner contends that the prior art teaches said limitations. Examiner contends that the Applicants “unexpected results of the stabilizers of the instant application providing unexpected improved results as compared to the stabilizers described in the prior art" is not unexpected and are obvious over the prior art of Torrens, in view of Kouzuma as Kouzuma teaches when a stabilizer such as sugar alcohol (same as ethylene glycol) is added to an enzyme reacting with a glycated amino acid, a surprisingly high stabilization effect to a degree that almost no decrease in the activity is seen when stored in a liquid state for four days at 37°C (Kouzuma: para 0029)
The rejection of claim 54 under 35 U.S.C. 103 as being unpatentable over Torrens et al (US Patent No: 6,008,006, Date of Patent: Dec. 28, 1999, cited on PTO-892 dated 1/24/2025) {herein Torrens} in view of Kouzuma et al (US Patent Application No: US 2005/0101771 A1, Date of Publication: May 12, 2005, cited on IDS filed on 2/11/2022) {herein Kouzuma} as applied to claims 42, 44-47, 49-50, 56, 58-59, 61 and in further view of Joo et al (Date of Publication: April 2005, Enzyme and Microbial Technology, doi:10.1016/j.enzmictec.2005.01.002, cited on PTO-892 dated 1/24/2025) {herein Joo} is maintained. The rejection has been modified in view of Applicant’s Appeal Brief dated 6/22/2026.
Claim 54 is drawn to the glycated protein assay reagent according to any one of claims 42, 44, 46, 49 and 50, wherein the stabilizer of the protease is propylene glycol, and the concentration of the propylene glycol in the first reagent or the second reagent is from 7.5wt/vol% to 80wt/vol%.
The teachings of Torrens, in view of Kouzuma as applied to claims 42, 44-47, 49-50, 56, 58-59, 61 are set forth in the 103 rejection above.
However, Torrens, in view of Kouzuma does not teach the product of claim 54, wherein the stabilizer of the protease is propylene glycol, and the concentration of the propylene glycol in the first reagent or the second reagent is from 7.5wt/vol% to 80wt/vol%.
With respect to claim 54, Joo teaches 10% propylene glycol increases the half-life of proteins in general and protects the proteins from degradation (abstract).
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to apply the teachings of Torrens et al of a glycated protein assay reagent or combine the teachings of Kouzuma and Joo because Joo teaches propylene glycol increases the half-life of proteins and protects the proteins from degradation (abstract). Kouzuma teaches ethylene glycol can suppress a decrease in protease activity during storage, even in a liquid state (para 0154). Whereas Torrens teaches glycated protein assay reagents containing: a trinder (peroxidase), aminoantipyrene, protease (proteinase K) and ferrocyanide (column 9, lines 14-26).
One of ordinary skill in the art would be motivated to substitute the protease stabilizers taught by Kouzuma with the protease stabilizer taught by Joo (propylene glycol) based on the teachings of Torrens, Kouzuma and Joo because Joo teaches polyethylene glycol increases the half-life of enzymes and its sustainability in a reaction (abstract). Increasing the half-life of the proteases within the glycated protein assay would result in sustained reactivity and reduced deterioration of the protease. As such, one of ordinary skill in the art would be motivated to substitute the protease stabilizer taught by Joo with that taught by Kouzuma as doing so would result in a glycated protein assay with stable proteases that extends the activity of the proteases within the reagent and their half-lives and said stabilizer has significant potential as a good stabilizer of protease preparations (abstract). One of ordinary skill in the art knowing the benefit of maintaining protease activity in a reagent based on the teachings of Torrens, Kouzuma and Joo would have a reasonable expectation of success to substitute the protease stabilizers taught by Kouzuma (ethylene glycol) with the protease stabilizer taught by Joo (polyethylene glycol) because one of ordinary skill in the art would expect it to result in a reagent with efficient protease activity over the course of the assay and during storage of the reagent.
One of skill in the art would have a reasonable expectation of success to make and use the claimed protease stabilizer (polyethylene glycol) because Joo provides the teaching of 10% propylene glycol increases the half-life of proteins and protects the proteins from degradation (abstract). Whereas Torrens provides the teachings of protein assay reagents containing: a trinder (peroxidase), aminoantipyrene, protease (proteinase K) and ferrocyanide (column 9, lines 14-26). Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
The rejection of claim 55 under 35 U.S.C. 103 as being unpatentable over Torrens et al (US Patent No: 6,008,006, Date of Patent: Dec. 28, 1999, cited on PTO-892 dated 1/24/2025) {herein Torrens} in view of Kouzuma et al (US Patent Application No: US 2005/0101771 A1, Date of Publication: May 12, 2005, cited on IDS filed on 2/11/2022) {herein Kouzuma} as applied to claims 42, 44-47, 49-50, 56, 58-59, 61 and in further view of Fenyvesi et al (US Patent No: US 8,802,729 B2, Date of Patent: Aug. 12, 2014, cited on PTO-892 dated 1/24/2025) {herein Fenyvesi) is maintained. The rejection has been modified in view of Applicant’s Appeal Brief dated 6/22/2026.
Claim 55 is drawn to the glycated protein assay reagent according to any one of claims 42, 44, 46, 49 and 50, wherein the stabilizer of the protease is trimethylene glycol, and the concentration of the trimethylene glycol in the first reagent or the second reagent is from 40wt/vol% to 80wt/vol%.
The teachings of Torrens, in view of Kouzuma as applied to claims 42, 44-47, 49-50, 56, 58-59, 61 are set forth in the 103 rejection above.
However, Torrens in view of Kouzuma do not teach the product of claim 55, wherein the stabilizer of the protease is trimethylene glycol, and the concentration of the trimethylene glycol in the first reagent or the second reagent is from 40wt/vol% to 80wt/vol%.
With respect to claim 55, Fenyesi teaches about 0.1% to about 99% (column 8, lines 25-31) 1,3-propanediol enhances the stability of enzymes (abstract). Evidentiary reference of PubChem is cited to demonstrate that trimethylene glycol is synonymous with 1,3-Propanediol (page 1).
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to apply the teachings of Torrens et al of a glycated protein assay reagent or combine the teachings of Kouzuma and Fenyvesi because Fenyvesi teaches about 0.1% to about 99% (column 8, lines 25-31) 1,3-propanediol enhances the stability of enzymes (abstract) and use it as proteinase stabilizer Whereas Torrens teaches glycated protein assay reagents containing: a trinder (peroxidase), aminoantipyrene, protease (proteinase K) and ferrocyanide (column 9, lines 14-26).
One of ordinary skill in the art would be motivated to combine the teachings of Torrens, Kouzuma and Fenyesi because Fenyesi teaches 1,3-propanediol enhances the stability of enzymes (abstract). As such, one of ordinary skill in the art would be motivated to substitute the protease stabilizers taught Torrens and Kouzuma with the protease stabilizer taught by Fenyesi based on the teachings of Torrens, Kouzuma and Fenyesi as doing so would result in a protease and enzyme stabilizer that extends the activity of the proteases and enzymes in the reagent. One of ordinary skill in the art knowing the benefit of maintaining protease and enzymatic activity in a reagent based on the teachings of Torrens, Kouzuma and Fenyesi would have a reasonable expectation of success to substitute the protease stabilizer taught by Kouzuma (ethylene glycol) with the enzyme stabilizer taught by Fenyesi (1,3-propanediol) because one of ordinary skill in the art would expect the enzyme stabilizer taught by Fenyesi to result in a reagent with efficient protease and enzymatic activity over the course of the assay and during storage of the reagent.
One of skill in the art would have a reasonable expectation of success to make and use the claimed enzymatic stabilizer because Fenyesi provides the teaching of 0.1% to about 99% (column 8, lines 25-31) 1,3-propanediol enhances the stability of enzymes (abstract). Whereas Torrens provides the teachings of protein assay reagents containing: a trinder (peroxidase), aminoantipyrene, protease (proteinase K) and ferrocyanide (column 9, lines 14-26). Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
The rejection of claim 57 under 35 U.S.C. 103 as being unpatentable over Torrens et al (US Patent No: 6,008,006, Date of Patent: Dec. 28, 1999, cited on PTO-892 dated 1/24/2025) {herein Torrens} in view of Kouzuma et al (US Patent Application No: US 2005/0101771 A1, Date of Publication: May 12, 2005, cited on IDS filed on 2/11/2022) {herein Kouzuma} as applied to claims 42, 44-47, 49-50, 56, 58-59, 61 and in further view of Sigma (Date: December 6, 1998 (archive date obtained using wayback machine), cited on PTO-892 dated 1/24/2025) {herein Sigma} and Severson et al (European Patent Application No: EP162033A2, Date Published: 21. 11.85, cited on PTO-892 dated 1/24/2025) {herein Severson) is maintained. The rejection has been modified in view of Applicant’s Appeal Brief dated 6/22/2026.
Claim 57 is drawn to the glycated protein assay reagent according to any one of claims 42, 44, 46, 49 and 50, wherein the stabilizer of the protease is 2-carboxyphenylboronic acid, and the concentration of the 2- carboxyphenylboronic acid in the first reagent or the second reagent is from 0.2 wt/vol% to 10wt/vol%.
The teachings of Torrens, in view of Kouzuma as applied to claims 42, 44-47, 49-50, 56, 58-59, 61 are set forth in the 103 rejection above.
However, Torrens in view of Kouzuma do not teach the method of claim 57, wherein the stabilizer of the protease is 2-carboxyphenylboronic acid, and the concentration of the 2- carboxyphenylboronic acid in the first reagent or the second reagent is from 0.2 wt/vol% to 10wt/vol% (claim 57).
With respect to claim 57, Sigma teaches 2-carboxyphenylboronic acid is a type of boronic acid (page 1) which is a derivative of a boric acid as it is an organic chemical compound that features both a boronic acid group and a carboxylic acid group attached to a benzene ring.
However, Sigma does not teach the composition is from 0.2 wt/vol% to 10 wt/vol% (claim 57).
With respect to claim 57, Severson teaches 0.25-15% (page 1, line 30) of a boric acid improves the enzyme stability in detergent compositions (page 1, lines 10-12).
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to apply the teachings of Torrens et al of a glycated protein assay reagent to combine the teachings of Kouzuma, Sigma and Severson because Severson teaches 0.25-15% (page 1, line 30) of a boric acid improves the enzyme stability in detergent compositions (page 1, lines 10-12). Sigma teaches 2-carboxyphenylboronic acid is a type of boronic acid (page 1) which is a derivative of a boric acid. Kouzuma teaches ethylene glycol can suppress a decrease in protease activity during storage, even in a liquid state (para 0154). Whereas Torrens provides the teachings of protein assay reagents containing: a trinder (peroxidase), aminoantipyrene, protease (proteinase K) and ferrocyanide (column 9, lines 14-26).
One of ordinary skill in the art would be motivated to combine the teachings of Torrens, Kouzuma, Sigma and Severson because Severson teaches boric acid enhances the stability of enzymes within compositions against precipitation when stored at low temperature or under free-thaw conditions (page 19, lines 31-33). As such, said property would extend the storage period of compositions with enzymes as said enzymes would retain its activity for a long period of time, under storage conditions. Furthermore, boric acid has been found to provide improved enzyme stability within compositions (page 1, lines 10-12). As such, one of ordinary skill in the art would be motivated to combine the teachings of Torrens, Kouzuma, Sigma and Severson as doing so would result in a protease stabilizer that extends the activity of the proteases and enzymes in the reagent. One of ordinary skill in the art knowing the benefit of maintaining protease and enzymatic activity in a reagent based on the teachings of Torrens, Kouzuma, Sigma and Severson would have a reasonable expectation of success to substitute the protease stabilizer taught by Kouzuma (ethylene glycol) with the enzymatic stabilizer taught by Severson (2-carboxyphenylboronic acid) because one of ordinary skill in the art would expect the enzymatic stabilizer taught by Severson (2-carboxyphenylboronic acid) to result in a reagent with efficient enzymatic activity over the course of the assay and during storage of the reagent, since Severson teaches said property of the enzymatic stabilizer in detergents. Additionally, one of ordinary skill in the art would expect 2-carboxyphenylboronic acid to have the same activity as boric acid since Sigma teaches 2-carboxyphenylboronic acid is a type of boronic acid (page 1) and Severson teaches boronic acid is a type of boric acid (page 12, line 29).
One of skill in the art would have a reasonable expectation of success to make and use the claimed protease stabilizer because Severson provides the teaching of 0.25-15% (page 1, line 30) of a boric acid improves the enzyme stability in detergent compositions (page 1, lines 10-12). Sigma provides the teaching that 2-carboxyphenylboronic acid is a type of boronic acid (page 1), which is also a type of boric acid (Severson, page 13, line 29).. Whereas Torrens provides the teachings of protein assay reagents containing: a trinder (peroxidase), aminoantipyrene, protease (proteinase K) and ferrocyanide (column 9, lines 14-26). Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
Conclusion
Status of the claims
Claims 42, 44-47, 49-50, 54-59, 61 are pending,
Claims 62-64 stand withdrawn from consideration pursuant to 37 CFR 1.142(b).
Claims 1-41, 43, 48, 51-53, 60 , 65-67 are cancelled.
Claims 42, 44-47, 49-50, 54-59, 61 are rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ERICA NICOLE JONES-FOSTER whose telephone number is (571)270-0360. The examiner can normally be reached mf 7:30a - 4:30p.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath Rao can be reached at 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/ERICA NICOLE JONES-FOSTER/Examiner, Art Unit 1656
/MANJUNATH N RAO/Supervisory Patent Examiner, Art Unit 1656
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