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 .
Priority
The instant application is a continuation (Bypass Application) of PCT/JP22/23533, filed 6/10/2022. Applicant’s claim for the benefit of a prior-filed foreign application JP2021-099705, filed 6/15/2021, under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. Receipt is acknowledged of certified copies of the priority documents.
It is noted that an English language translation of application JP2021-099705 has not been made of record in accordance with 37 CFR 1.55. Thus, the claimed priority date cannot be relied upon to overcome any potential rejection of intervening art. When an English language translation of a non-English language foreign application is required, the translation must be that of the certified copy (of the foreign application as filed) submitted together with a statement that the translation of the certified copy is accurate. See MPEP §§ 215 and 216.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 4/14/2026, 1/18/2024, and 2/13/2023 are acknowledged. The submissions are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements have been considered by the examiner.
Election/Restrictions
Applicant’s election of Group I, claims 1-2, in the reply filed on 3/4/2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)). The election is still deemed proper and is made Final.
Claims 3-8 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected inventions, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 3/4/2026, as indicated above.
Claims 1 and 2 were examined on the merits herein.
Claim Interpretation
The term “mediator” is being interpreted under the broadest reasonable interpretation (B.R.I.), in light of the specification and in view of the meaning of the term in the art.
The specification, at [0058], describes the mediator as being a reduced mediator, also referred to as a proteinaceous mediator, an artificial electron mediator, an artificial electron acceptor, or an electron mediator that is to be used in the quantitation method, and this is not particularly limited as long as it can supply electrons to the hydroxylase. Examples provided for the mediator in the disclosure include quinones, phenazines such as safranins, viologens, cytochromes, phenoxazines such as nile blue, phenothiazines, ferricyanides such as potassium ferrocyanide, ferredoxins, isoalloxazines such as riboflavin, ferrocene, syringaldazine, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), osmium complexes, ruthenium complexes, and derivatives thereof. From reviewing the art, it is clear that one of ordinary skill in the art would be readily knowledgeable of suitable reduced mediators that provide electrons to the reaction.
Therefore, under the B.R.I., the mediator is being interpreted as any suitable substance that provides electrons to the reaction for the hydroxylase to act upon 25-hydroxyvitamin D.
Claim Objections
Claim 2 is objected to because of the following informalities:
Claim 2 recites: “comprising: quantifying an oxidized mediator produced by an action of the hydroxylase, or oxygen or a reduced mediator consumed by an action of the hydroxylase”, in lines 2-5. The metes and bounds of the claim can be understood from the description in the specification- e.g. this is reciting monitoring the consumption of the alternatives oxygen or a reduced mediator- however the language is imprecise due to the repeated use of “or” without commas or other clarification of the method step. It is recommended that this claim limitation is amended to recite the following:
“further comprising:
a) quantifying an oxidized mediator produced by an action of the hydroxylase; or
b) quantifying a loss of oxygen or a reduced mediator consumed by an action of the hydroxylase.”
Appropriate correction is required.
Claim Rejections - 35 USC § 112(a) - Written Description
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1 and 2 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement.
The claims contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 1 recites a method for quantifying 25-hydroxyvitamin D comprising: adding a mediator and hydroxylase to a sample. Claim 2 does not practically limit the encompassed hydroxylase. The claims thus encompass any hydroxylase, a large genus of enzymes.
According to the B.R.I. of the claim, when viewed in light of the specification, there exists a nearly limitless number of hydroxylase enzymes (all those known in the art and yet-to be discovered) within the claimed scope. Comparatively, the specification only recites a small number of species of the broad genus that meets the recited limitations.
MPEP § 2163.(II)(A)(3)(a) states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the inventor was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
The specification fails to reasonably describe the full genus of the claimed invention by providing identifying characteristics or functional properties of the claimed hydroxylases.
The instant specification does not disclose relevant identifying characteristics, such as key structural or other physical properties, e.g. a sequence motif or physical structure considered to be an active site. Further, the disclosure does not adequately describe functional characteristics coupled with a known or disclosed correlation between function and the structure or sequence, such that the entirety of the claimed genus is encompassed by the description in the disclosure.
The disclosure states that among the hydroxylases belonging to E.C. 1.14., an enzyme that recognizes 25- hydroxyvitamin D as a substrate and has 25-hydroxyvitamin D hydroxylase activity can be used as the hydroxylase ([0024]). However, E.C. 1.14.-.- encompasses all oxidoreductases that act on paired donors with incorporation or reduction of molecular oxygen (“Expasy ENZYME class: 1.14.-.-”, accessed at purl.expasy.org/enzyme/EC/1.14.-.-).
However, it is apparent from the art that vitamin D 25-hydroxylases belong to E.C. 1.14.14.24, which encompasses oxidoreductases, with reduced flavin or flavoprotein as one donor and incorporation of one atom of oxygen, e.g. hydroxylases, which act upon 25-hydroxyvitamin D (e.g. “Expasy ENZYME class: 1.14.14.24”, accessed at purl.expasy.org/enzyme/EC/1.14.14.24).
The specification describes a hydroxylase derived from a Pseudonocardia autotrophica NBRC12743 strain as an exemplary hydroxylase, but states that the present invention is not limited to this ([0024], [0027]). This hydroxylase has the amino acid sequence of SEQ ID NO: 1, and may be encoded by a nucleotide having the base sequence shown in SEQ ID NO: 2 ([0027]-[0028]). However this is a description of a single embodiment of the claimed genus, and there is no known or disclosed relationship between the sequence and function that is sufficient to fulfill the written description requirement.
There appear to be only a handful of enzymes having hydroxylase activity with 25-hydroxyvitamin D as the substrate known in the art.
Zhu & DeLuca (2012. “Vitamin D 25-hydroxylase–four decades of searching, are we there yet?”. Archives of biochemistry and biophysics, 523(1), 30-36. DOI: 10.1016/j.abb.2012.01.013) is a review that discusses processes for bioactivation of vitamin D3, including 25-hydroxylation and the subsequent 1α-hydroxylation to produce 1α,25-dihydroxyvitamin D3 [1,25(OH)2D3], the active hormone (Abstract). Zhu & DeLuca discuss six cytochrome P450 enzymes (CYP27A1, CYP2R1, CYP2J2/3, CYP3A4, CYP2D25 and CYP2C11) involved in the initial 25-hydroxylation step (Abstract). Zhu and DeLuca also discuss that CYP27B1 is believed to be the sole 25(OH)D3 1α-hydroxylase in human tissues (Fig. 2, Page 30, left col.). Thus this references establishes that, in humans, there are multiple vitamin D 25-hydroxylases, depending on the tissue (Table 1), and a single 1a-hydroxylase (CYP27B1), which is capable of acting upon 25-hydroxyvitamin D (Fig. 2).
Fujii et al. (2009. “Purification, characterization, and directed evolution study of a vitamin D3 hydroxylase from Pseudonocardia autotrophica”. Biochemical and Biophysical Research Communications 385: 170–175, DOI: 10.1016/j.bbrc.2009.05.033) discusses a hydroxylase from the actinomycete Pseudonocardia autotrophica which is capable of bioconversion of VD3 into 25(OH)VD3 and sequentially acts upon 25(OH)VD3 to yield 1α,25-(OH)2VD3 (Title, Abstract, Fig. 3). Fujii discusses the purification and characterization of Vdh (vitamin D3 hydroxylase) from P. autotrophica strain NBRC12743 (Fig. 1, Table 1).
On the other hand, Abdulmughni et al. (2017, “Biochemical and structural characterization of CYP109A2, a vitamin D3 25-hydroxylase from Bacillus megaterium.” FEBS J, 284: 3881-3894. DOI: 10.1111/febs.14276) teaches the enzyme CYP109A2, a vitamin D3 25-hydroxylase from Bacillus megaterium, that catalyzes the hydroxylation of vitamin D3 to its 25-hydroxylated derivative with high regio-selectivity, and using ferredoxin, Fdx2 (Abstract, Fig. 6). There is no indication of the production of 1a,25(OH)2-VD3 in this study. It is evident that not every vitamin D hydroxylase has the activity of acting upon 25-hydroxyvitamin D, which is necessary in the instant method to quantify 25-hydroxyvitamin D.
Further, the working examples in the instant disclosure only disclose a method using the VDH gene derived from Pseudonocardia autotrophica strain NBRC12743, which is described in Fujii et al., the enzyme having the amino acid sequence of SEQ ID NO:1 (see [0079]-[0098]). Because the specification only provides only 1 example of the claimed genus of hydroxylase enzymes, this cannot be considered a sufficient description of a representative number of species by actual reduction to practice of the full breadth of the vast genus.
There is no evidence that, at the time of filing, the Applicant possessed additional representative species of the full genus recited in the claims beyond those provided in the working examples. For these reasons, the disclosure fails to provide adequate written description to support the entirety of the broad genus claim to any and all hydroxylases.
Claims 1 and 2 are thus rejected under 35 U.S.C. § 112(a) because the claimed subject matter is not described in the specification in such a way as to reasonably convey to a skilled artisan that the inventor, or a joint inventor, had possession of the claimed invention.
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 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 2 are rejected under 35 U.S.C. 103 as being unpatentable over Ludwig et al. (WO2010014978A1, herein after “Ludwig”) in view of Urushino et al. (2006. “Interaction between mitochondrial CYP27B1 and adrenodoxin: role of arginine 458 of mouse CYP27B1”. Biochemistry, 45(14), pp.4405-4412, herein after “Urushino”).
Ludwig teaches a method for determining the amount of hydroxyvitamin D3, including methods for quantifying the amounts of 25(OH)D and its derivative 1,25-dihydroxy Vitamin D using a hydroxylase (Abstract, Fig. 1, page 5, lines 4-30, cited below).
“ "Bio-electrode" is, broadly, an electrode that functions as an interface between biological structures and electronic systems, the present system the electrode comprises recombinant lα-hydroxylase (i.e., CYP27B1). CYP27B1 catalyzes the conversion of 25-hydroxy Vitamin D. During the catalysis, an electrical signal so generated is measured and calibrated against known concentrations. An lα-hydroxylase (CYP27B1) is a heme-containing monooxygenase that accepts two electrons and reduces on atom of 02 to water, inserting the other oxygen atom onto the substrate. Electrons can be transferred directly to CYP27B1, eliminating the need for components of the in vivo electron transport system. In vitro electrons can be supplied catalytically, with the catalytic current directly proportional to the amount of 25(OH)D.
"Biological material" shall be broadly understood to mean blood, serum, tears whether in vivo or in vitro.
Referring now in particular to FIG. 1, the invention relates to a biosensor comprising a device for measuring vitamin D concentration comprising an enzyme based working electrode and a means of measuring an electrical signal generated at the electrode. The electrode (which in one exemplary embodiment represents a working electrode WE shown in FIG. 2) includes recombinant lα-hydroxylase (CYP27B1). This enzyme catalyzes the conversion of 25-hydroxy Vitamin D to its active form 1,25-dihydroxy Vitamin D. During the catalysis, the electrical signal generated will be measured by the measuring means and calibrated against known concentrations. CYP27B1 is a heme-containing monooxygenase that accepts two electrons and reduces one atom of 02 to water, inserting the other oxygen atom onto the substrate. In vitro, electrons can be supplied catalytically, with the catalytic current directly proportional to the amount of 25(OH)D.”
Ludvig also teaches immobilizing P450s such as CYP27B1 onto the electrodes, with various methods known to the art (pages 6-7), and discloses producing DDAB/EPG electrodes with purified CYP27B1 and used the electrodes for measuring 25-hydroxyvitamin D3 (pg 9, lines 10-30).
Ludvig thus teaches a method for using a hydroxylase, particularly lα-hydroxylase (i.e., CYP27B1) for detecting the amount of 25(OH)D with an electrode (see e.g.) .
However, Ludvig does not explicitly teach adding a mediator to the reaction, nor a measurement of an oxidized mediator, oxygen, or a reduced mediator, as recited in claim 2.
Urushino pertains to studies of the hydroxylase CYP27B1 and its interaction with adrenodoxin (ADX) (Abstract, Title). Urushino teaches that ADX functions as an effector for the oxygen transfer reaction in addition to being an electron donor for CYP27B1 (Abstract, last line).
Urushino teaches that “On the inner membrane of the mitochondria, all mitochondrial P450s interact with a common electron donor, ADX, which is an acidic [2Fe-2S] ferredoxin-type protein” (pg. 4405, left col.) Urushino also teaches that ADX affects the catalytic activity of wild-type CYP27B1 in a dose-dependent manner (Fig. 6A, and pg. 4410, left col).
Regarding claim 2, Urushino teaches that ADX functions as an electron carrier between a FAD-containing NADPH-dependent adrenodoxin reductase (ADR) and the cytochrome P450 (e.g. CYP27B1 in this case). Urushino describe quantitative assays for CYP27B1 activity with 25(OH)D as the substrate, wherein the assays detect changes in the amount of NADPH (e.g. a reduced mediator), using spectrometry (see e.g. the method sections “Measurement of the NADPH-Dependent Reduction Rate of CYP27B1 and Its Mutants” and “Measurement of Consumption of NADPH during 1R Hydroxylation of 25(OH)D3”, both on page 4407).
Thus, Urushino teaches that adrenodoxin (ADX), a ferredoxin-type protein, acts as a mediator for the conversion of 25(OH)D to 1,25-dihydroxy Vitamin D, and teaches reacting 25(OH)D with adrenodoxin (ADX), NADPH-dependent adrenodoxin reductase (ADR), and NADPH (of which the consumption is detectable with known spectrometry methods).
Therefore, to one of ordinary skill in the art, before the effective filing date of the instant invention, it would have been prima facie obvious to improve upon the CYP27B1 hydroxylase-based detection method of Ludvig by incorporating the reaction mediator adrenodoxin (ADX) taught in Urushino, for the predictable benefit of increasing the catalytic turnover of the hydroxylase and thus the sensitivity and efficiency of the detection of 25(OH)D.
One would have been motivated by the teachings of Urushino to add an effector such as adrenodoxin (ADX) that increases the catalytic activity of CYP27B1, because doing so would increase the effectiveness of the enzyme reaction. Such optimization of enzyme based detection is common in the art. Further, one of ordinary skill in the art would recognize that with improved reaction kinetics, less enzyme can be used for the sensor, and this will enable detection of smaller amounts of the target substrate, 25(OH)D (e.g. increased sensitivity). MPEP § 2143.II.C (relating to exemplary KSR Rationale C) which discusses it is obvious to use a known technique to improve similar devices (methods, or products) in the same way, when the result would be predictable to one of ordinary skill. From the combined teachings of Urushino and Ludvig, it is predictable that the addition of the redox mediator adrenodoxin (ADX) would improve the reaction efficiency of the detection method using CYP27B1. See MPEP §§ 2144.I and 2144.II.
Regarding claim 2, one having ordinary skill would be knowledgeable in various means for measuring reactions and thus determining the amount or detecting the level of the target substrate, 25(OH)D. Urushino teaches measuring CYP27B1 activity using a reaction with adrenodoxin (ADX), ADR, and NADPH, wherein the consumption of NADPH is monitored with a change in absorbance. Using spectroscopy to determine the starting concentration of the target compound, when the concentrations of the other components are known, would have been obvious to one of ordinary skill because measuring reduced substrates (e.g. NADPH) is a common technique in the art, and such assays are taught in Urushino. Further, measuring the change in electric current as taught in Ludvig is indirectly a method for measuring the consumption rate of oxygen in the sample used therein, as the transfer of oxygen to the target substrate is what generates the difference in electrical potential. To one having ordinary in this art, the method of detection would be a manner of judicial selection or routine optimization.
From the combined teachings of Ludvig and Urushino, it is apparent that there would have been a reasonable expectation of success in combining the teachings therein to arrive at the instantly claimed invention because both references pertain to studying the reaction of the reductase CYP27B1 with 25(OH)D3, Ludvig teaches reacting 25(OH)D3 with CYP27B1 to detect 25(OH)D3 and its product 1,25(OH)D3, and Urushino teaches mediators that improve the reaction kinetics of 25(OH)D3 and CYP27B1.
Therefore, the invention as a whole would have been prima facie obvious to one of ordinary skill in the art prior to the effective filing date, as evidenced by the cited references, especially in the absence of evidence to the contrary.
Claims 1 and 2 are rejected under 35 U.S.C. 103 as being unpatentable over Sakaki et al. (2016 “Advanced use of vitamin D hydroxylases.” Final research report of Grants-in-Aid for Scientific Research (online). URL: https://kaken.nii.ac.jp/report/KAKENHI-PROJECT-25292062/25292062seika/, of record, cited on IDS filed 12/13/2023: see the English language translation included therein) in view of Fujii (US PGPub No. 20100297712, cited on IDS filed 12/13/2023).
Sakaki teaches a method for measuring the amount of 25-hydroxyvitamin D, 25(OH)D, in blood (for evaluating the risk of diseases such as osteoporosis) using a vitamin D hydroxylase (Title, Background). Sakaki teaches a measurement system using an electrode to which vitamin D hydroxylase was immobilized (section 1, last line). Sakaki teaches using various membrane bound cytochrome P450 reductases (translated section 3, e.g. CYP3A4, CYP21A2, CYP105A).
However, Sakaki does not teach a quantification method for 25-hydroxyvitamin D using a hydroxylase and a mediator, as required in the instant claims.
Fujii teaches a hydroxylase from Pseudonocardia autotrophica- NBRC12743 strain, that performs hydroxylation at the 1α and 25- positions of vitamin D3 (Abstract, [0024]). Fujii teaches that 25-hydroxy vitamin D3 is a substrate for the hydroxylase from P. autotrophica, termed VDH (vitamin D hydroxylase) (see [0050], , Fig. 8- lower graph). Fujii teaches that VDH has high hydroxylation activity at both the 25-position of vitamin D3 and at 1α-position of 25-hydroxyvitamin D3 ([0083]-[0084], Table 2).
Fujii teaches a gene encoding VDH and the amino acid sequence for VDH, which are the sequences defined in sequence No. 1 and sequence No. 2, respectively ([0060], [0069]). Sequence No. 2 in Fujii is identical to the instantly recited amino acid sequence of SEQ ID NO: 1 (see the sequences on pages 15-18 of Fujii).
Regarding the mediator, and the limitations of claim 2, Fujii teaches that to show hydroxylation activity, it is preferable to coexpress VDH and the gene coding redox partner proteins which are capable of transferring electrons efficiently to VDH, including ferredoxin and ferredoxin reductase ([0064], [0076]-[0078]). Fujii teaches that the redox mediator (or redox partner) may be ferredoxin and ferredoxin reductase, derived from spinach, or derived from Acinetobacter sp. OC4 and/or Rhodococcus erythropolis ([0077] and claim 13). In examples, Fujii teaches testing VDH activity and kinetics with ferredoxin and ferredoxin reductase derived from spinach, and adding the redox cofactors NADH and NADPH (Example 11, [0123]).
Thus, to one of ordinary skill in the art, before the effective filing date of the instant invention, it would have been prima facie obvious to modify the measurement system and methods comprising a sensor or electrode using vitamin D hydroxylase taught in Sakaki by selecting the hydroxylase from Pseudonocardia autotrophica- NBRC12743 taught in Fujii, for the predictable benefit of detecting vitamin D and 25-hydroxyvitamin D in samples, and it would have been obvious to provide mediators including ferredoxin and ferredoxin reductase and the cofactors NADH and/or NADPH when doing so, to facilitate electron transport.
One would have been motivated to select the VDH hydroxylase because it can act upon both vitamin D and 25-hydroxyvitamin D, and thus, one would predict that this enzyme can be used to detect 25-hydroxyvitamin D, a predominant circulating vitamin D derivative in blood (see e.g. [0004] of Fujii). Fujii demonstrates the kinetic activity of VDH, and thus to one of ordinary skill in the art it would have been predictable that providing this enzyme in a Vitamin D detection assay, such as the one taught in Sakaki, would result in improved sensitivity. Further, the incorporation of one or more of the mediators taught in Fujii would have been obvious, because these are known redox mediators, necessary to enable the function of cytochrome p450 enzymes, and their presence would predictably increase the activity of the hydroxylase.
Regarding claim 2, detecting the hydroxylase activity by monitoring a change in the amount of oxidized mediator or a reduced mediator is known in the art, as indicated in Sakaki by testing for changes in electrical current, when the enzyme reacts with a substrate (thus indirectly measuring changes in redox potential of the mediators).
From the combined teachings of Sakaki and Fujii, it is apparent that there would have been a reasonable expectation of success in combining the teachings therein to arrive at the instantly claimed method for detecting 25-hydroxyvitamin D, because both pertain to vitamin D hydroxylases and both references suggest monitoring vitamin D derivatives such as 25-hydroxyvitamin D for detecting diseases in subjects.
Therefore, the invention as a whole would have been prima facie obvious to one of ordinary skill in the art prior to the effective filing date, as evidenced by the cited references, especially in the absence of evidence to the contrary.
Citation of Pertinent Art
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
St-Arnaud et al. (US Pat. No. 6,096,876) pertains to polynucleotides encoding all or a fragment of the P450 moiety of vitamin D 1α-Hydroxylase and teaches that such polypeptides are used in methods of diagnosing and treating vitamin D-related disorders and of producing vitamin D metabolite (Abstract, Claim 1). St. Arnaud et al. teaches that the conversion of 25(OH)D to 1α,25(OH)2 D3 is catalyzed by the described 25-hydroxyvitamin D- 1α-hydroxylase, a renal cytochrome P450 enzyme of the vitamin D pathway (Col 1, lines 25-44).
Conclusion
Claims 1 and 2 are rejected. No claims are allowable.
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/A.T.M./Examiner, Art Unit 1655
/ANAND U DESAI/Supervisory Patent Examiner, Art Unit 1655
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