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 .
Status of Application, Amendments and/or Claims
The amendment, filed 03 June 2022, has been entered in full. Claims 6, 9, 11, and 12 are amended.
Applicant’s election without traverse of Group III (claims 6-12) in the reply filed on 19 May 2026 is acknowledged.
Claims 1-5 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected Group, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 19 May 2026.
Claims 6-12 are under examination.
Foreign Priority
Acknowledgment is made of Applicant's claim for foreign priority under 35 U.S.C. 119(a)-(d). The certified copy JP 2019-221264 (filed 12/6/2019) and 371 of PCT/JP2020/041874 (11/10/2020) have been placed of record in the file.
Information Disclosure Statement
The information disclosure statement(s)(IDS) (filed 8/30/2022 and 3/6/2024) were received. They have been placed in the application file and the information referred to therein has been considered as to the merits.
It is noted that one of the references fails to comply with the provisions of 37 CFR §§1.97, 1.98 and MPEP § 609. MPEP 609.05 [R-3] states that information disclosure statements will be reviewed for compliance with the requirements of 37 CFR 1.97 and 37 CFR 1.98 as discussed in MPEP 609.04(a) and MPEP 609.04(b). The references will be lined through and not considered by the Examiner.
The following reference not considered by the Examiner for the following reasons:
The Narimatsu reference (submitted on the IDS 8/30/2022) is not being considered by the Examiner because the reference is in a language other than English and does not have an English abstract.
Applicant is advised that the date of any re-submission of any item of information contained in this information disclosure statement or the submission of any missing element(s) will be the date of submission for purposes of determining compliance with the requirements based on the time of filing the statement, including all certification requirements for statements under 37 CFR 1.97(e). See MPEP § 609.05(a).
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 6-12 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.
Claim 6 is indefinite because it depends from a withdrawn claim.
Claim 6 is indefinite because the entire scope of the claim is unclear. For example:
What tool or assay is being used to measure PSA?
What is the “signal” coming from/derived from PSA in the sample?
How is the signal “converted” into a quantitative result?
It is unclear if the PSA in the sample is actually being compared to a reference sample?
It is unclear what is meant by “the relationship between the obtained signal and the predetermined concentrations is used at the quantitative information”?
Claim 6 is indefinite because it does not clearly differentiate between “PSA in a sample”, “PSA of interest” , “PSA with a sugar chain represented by any of formulae A to D” and “standard substance”. For example:
Is “PSA in the sample” the same as “PSA of interest”?
Is the “PSA with a sugar chain represented by any of formulae A to D” considered the reference PSA”.
How does the “reference sample” differ from “the standard substance”?
Claims 7-12 are included in this rejection insofar as they depend from claim 6 and do not resolve the issue discussed above.
Claim 12 is indefinite because it lacks antecedent basis for “the lectin and the antibody”.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 12 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 12 recites, “the method for quantifying PSA according to claim 7, wherein the lectin and the antibody are used as secondary capture molecules for the ligand binding assay”.
The claim does not further limit claim 7 because it does not recite the “primary capture molecules” for the ligand binding assay.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 112
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 6-12 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 claim(s) 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.
The instant claims are drawn to a method for quantifying PSA. In order to evidence possession of the claimed method, one would need to demonstrate possession of the claimed process steps which require the use of undisclosed molecules.
The method requires the use of undisclosed capture molecules. In particular, the method requires lectin capture molecules with the biological function of having “affinities for PSA having ß-N-acetylgalactosamine residue at a terminal of the sugar chain that are higher than that for PSA not having ß-N-acetylgalactosamine residue at any terminal of the sugar chain”.
The method also requires antibody capture molecules with the biological function of having “affinities for PSA having ß-N- acetylgalactosamine residue at a terminal of the sugar chain that are higher than that for PSA not having ß-N-acetylgalactosamine residue at any terminal of the sugar chain”.
MPEP § 2163 states: the written description requirement for a claimed genus may be satisfied through establishment of a structure-function correlation (show a structure is correlated with the function) OR through a sufficient description of a representative number of species (show a representative number of species that have the function. There must be enough species that are representative of the full breadth of the genus).
Regarding structure-function correlation of lectins: The claim is drawn to a genus of lectin capture molecules based entirely on the function of having affinity for PSA with a ß-N- acetylgalactosamine residue at a terminal of the sugar chain.
There is no disclosure of a correlation between a lectin structure and the claimed function. The number of structures encompassed by the genus may be vast or conversely there may be no structures that possess the claimed function. The disclosure fails to describe the common attributes or characteristics that identify the members of the genus. The instant claims do not limit the number of modifications that can be made in the lectin. It is in no way predictable that randomly selected changes in the disclosed sequence would afford a lectin protein having activity comparable to the one disclosed. For sequences having one or two substitutions, for example, the artisan would reasonably expect that many of the possible variants would retain functional properties comparable to those of the unmodified lectin protein, and it would require only routine manipulations to make and test a reasonably representative sampling of the possible variants. However, as the number of modified sites increases, the number of possible variants, and hence the degree of experimentation required, increases exponentially. Additionally, as plural substitutions are introduced, their interactions with each other and their effects on the structure and function of the protein become progressively less predictable.
Bhattacharya et al. state that the range of possible effects of even single nucleotide variations at the protein level are significantly greater than currently assumed by existing software prediction methods, and that correct prediction of consequences remains a significant challenge (p. 18)(Bhattacharya et al. Impact of genetic variation on three dimensional structure and function of proteins PLoS ONE 12(3): e0171355; 2017).
Fenton et al. state that while it is well known that most substitutions at conserved amino acid positions (which they call “toggle” switches) abolish function, it is also true that substitutions at non-conserved positions (which they call “rheostat” positions) are equally capable of affecting protein function. They conclude that substitutions at rheostat positions have highly unpredictable outcomes on the activities and specificities of protein-based drugs (see entire reference: Rheostat positions: A new classification of protein positions relevant to pharmacogenomics Medicinal Chemistry Research 29:1133-1146; 2020). The level of skill and knowledge in the art is such that one of ordinary skill would not be able to identify without further testing which of those lectins have the claimed activity.
Regarding structure-function correlation of antibodies: the art recognizes that the formation of an intact antigen-binding site of all antibodies requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs or hypervariable regions, which provide the majority of the contact residues for the binding of the antibody to its target epitope (see entire reference: Al Qaraghuli et al. Antibody-protein binding and conformational changes: identifying allosteric signaling pathways to engineer a better effector response. Nature Scientific Reports 10:13969, 2020).
Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences, and representative of almost the entire extensive heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines), and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well (see entire reference: The remarkable flexibility of the human antibody repertoire; isolation of over one thousand different antibodies to a single protein, BLyS. Journal of Molecular Biology 334:103-118; 2003).
Additionally, even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function. Rudikoff et al. teach that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function (Rudikoff et al. Single amino acid substitution altering antigen-binding specificity Proc. Natl. Acad. Sci. USA, 79(6):1979-1983, March 1982). The combination of evidentiary publications thus underscores a lack of structure-function correlation in antibody molecules.
Regarding a representative number of species: the instant specification fails to describe a representative number of species to provide adequate written description of the claimed genus as per MPEP § 2163. There must be enough species that are representative of the full breadth of the genus.
Species of lectins: the specification teaches Wisteria floribunda agglutinin (WFA), soybean agglutinin (SBA), Vicia villosa lectin (VVL), or Trichosanthes japonica agglutinin (TJA-II) (para 0040). However, the specification only teaches that WFA has the claimed affinity function (see para 0005).
Species of antibodies: the specification teaches anti-α-fetoprotein (AFP) monoclonal antibody, an anti-carcinoembryonic antigen (CEA) monoclonal antibody, anti-CA19-9 monoclonal antibody, and anti-PSA monoclonal antibody (para 0205).
However, there is no teaching that any of these antibodies have the claimed function of having “affinities for PSA having ß-N-acetylgalactosamine residue at a terminal of the sugar chain that are higher than that for PSA not having ß-N-acetylgalactosamine residue at any terminal of the sugar chain”.
The disclosed lectins and antibodies are not representative of an entire genus of lectin and antibodies comprising an unlimited number of different structures with the claimed function having “affinities for PSA having ß-N-acetylgalactosamine residue at a terminal of the sugar chain that are higher than that for PSA not having ß-N-acetylgalactosamine residue at any terminal of the sugar chain”.
The courts have specifically stated that the skilled artisan cannot envision the detailed chemical structure of an encompassed polypeptide until the structure is disclosed, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483. In Fiddes, claims directed to mammalian FGF' s were found to be unpatentable due to lack of written description for that broad class. The specification provided only the bovine sequence.
Therefore, the claim does not meet the written description provision of 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph.
.
Claim Rejections - 35 USC § 102
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 the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
1. Claims 6, 7, 9, 10 and 12 are rejected under 35 U.S.C. 102(a1) as being anticipated by Tabares et al. (Reference submitted by Applicant; Glycoprotein Volume 16:132-142, 2006).
Tabares et al. teach that differences in the glycosylation of PSA derived from prostate cancer (PCa) patients’ sera, seminal plasma, and LNCaP cells (a tumor prostate cell line) were established by lectin detection, glycosylation immunosorbent assay, and two-dimensional electrophoresis. Tabares et al. teach comparing the glycans released from the total glycoproteins (abstract).
Tabares et al. teach distinctive features between PSA from PCa patient serum, in relation to seminal plasma, could be attributed to differences in Fuc and GalNAc content. In PCa, the fucosylated structures are greatly reduced and GalNAc structures are not detectable. Tabares et al. teach in seminal plasma, GalNAc structures are clearly present (page 133, right column, last paragraph). Tabares et al. teach a PSA glycan structure (page 136, Table 1 FcA2G1GN1). The structure taught by Tabares is the same structure recited in claim 1 (Formula 1, A Galβ1–4GlcNAc )(applies to claim 6).
Tabares et al. teach that the difference between PSA glycans from a prostate cancer (PCa) patient serum and PSA glycans from seminal plasma is useful for distinguishing between normal PSA and tumor PSA. Tabares et al. teach that the amount of pure PSA needed for glycan sequencing requires large serum volumes and several purification steps, so they developed different methods to characterize and study PSA glycans from PCa patients’ sera.
Glycan characterization of PSA is carried out using lectins. Tabares et al. teach that before lectin characterization, sera was treated either by immunoprecipitation or by thiophilic absorption to increase the concentration of PSA in relation to the other serum proteins present. Three immunosorbed PSA samples (from seminal plasma, from a PCa patient serum and secreted by the PCa cell line LNCaP) were compared by western blotting using lectins Sambucus nigra (SNA), Mackia amurensis (MAA), Aleuria aurantia (AAL) and Erithrina cristagalli lectin (ECL)(page 135 and Figure 4)(applies to claims 6 and 7). Tabares et al. teach the employed antibodies and lectins are labeled with a fluorescent dye. Tabares et al. teach primary and secondary capture molecules for the ligand binding assays (page 137, 3rd full paragraph and page 141, left column, 3rd paragraph-page 143)(applies to claims 10 and 12).
Tabares et al. teach that lectin ECL strongly recognizes the Galβ1–4GlcNAc epitope and it is more abundant in PSA from a PCa patient serum than in PSA from seminal plasma, which presented more GalNAc in its terminal oligosaccharide structures. Tabares et al. teach that ECL detection by western blotting or ELISA, therefore, allowed PSA of PCa A serum to be distinguished from that of seminal plasma (page 140, lines 11-17 and Figure 5a)(applies to claim 9).
2. Claims 6-12 are rejected under 35 U.S.C. 102(a1) and 35 U.S.C. 102(a2) as being anticipated by Hirano et al. (US 20110236995, published Sept 29, 2011) as evidenced by Hirano et al. (Expression of LacdiNAc Groups on N-Glycans among Human Tumors Is Complex. BioMed Research International. Volume 2014, 7 pages).
Hirano et al. teach that the present invention provides a method for detecting a glycan structure of a prostate specific antigen (PSA) rapidly and with high sensitivity and determining prostate carcinoma based on the difference in the structure. Hirano et al. teach a method for determining between prostate carcinoma and benign prostatic hyperplasia accurately.
Hirano et al. teach a method for determining prostate carcinoma, wherein the method includes a step of analyzing a PSA glycan structure in a sample derived from a test subject. Hirano et al. teach prostate carcinoma is determined in the case that the amount of a glycan having N-acetylgalactosamine-N-acetylglucosamine (LacdiNAc(+)) is more than 30% of amount of a glycan not having LacdiNAc but having LacNAc (galacotose-N-acetylglucosamine) (LacdiNAc(-)). Hirano et al. teach a method for determining prostate carcinoma, wherein prostate carcinoma is determined in the case that amount of a glycan having LacdiNAc (N-acetylgalactosamine-N-acetylglucosamine) (LacdiNAc(+)) is more than 30% of amount of a glycan not having LacdiNAc but having LacNAc (galacotose-N-acetylglucosamine) (LacdiNAc(-)), and benign prostatic hyperplasia is determined in the case of 30% or less (abstract).
The N-acetylgalactosamine-N-acetylglucosamine (LacdiNAc(+)) structure taught by Hirano (for example chemical formula 1b, chemical formula 3f and chemical formula 4l) is the same structure recited in instant claim 1 (Formula 1, A Galβ1–4GlcNAc)(applies to claim 6).
LacdiNAc has the chemical name and structure GalNAcβ1–4GlcNAc, as evidenced by Hirano et al. (abstract and page 1)(Hirano et al. BioMed Research International. Volume 2014, 7 pages)(applies to claim 6).
Hirano et al. teach for detection, using a lectin or an antibody, that is bonded to an enzyme such as alkaline phosphatase and horseradish peroxidase, chemical color production using bromochloroindolyl phosphoric acid (BCIP) or nitroblue tetrazolium (NBT) via an enzymatic reaction, or chemical luminescence using a luminol reagent, or surface plasmon resonance may be used. In a related matter, the detection object is bonded to an immobilized specifically bonding molecule; and then a series of detection may be carried out by reacting the bonded object with a different kind of a specific lectin or a specific antibody (para 0102)(applies to claims 6-8, 10 and 12). Hirano et al. teach that in the case that a lectin is used as the specifically bonding molecule, the LacdiNAc(+) glycan may be detected by a wisteria floribunda agglutinin (WFA) lectin, capable of recognizing a non-reduced GalNAc terminal, to PSA. In the case that an antibody is used as the specifically bonding molecule, commercially available polyclonal antibody or monoclonal antibody may be used as the antibody to PSA (para 0103)(applies to claims 9 and 11).
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.
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 6-12 are rejected under 35 U.S.C. 103 as being unpatentable over Tabares et al. (Glycoprotein Volume 16:132-142, 2006) in view of Yamashita et al. (US 2016/0305960; published October 20, 2016).
Tabares et al. teach that differences in the glycosylation of PSA derived from prostate cancer (PCa) patients’ sera, seminal plasma, and LNCaP cells (a tumor prostate cell line) were established by lectin detection, glycosylation immunosorbent assay, and two-dimensional electrophoresis. Tabares et al. teach comparing the glycans released from the total glycoproteins (abstract). Tabares et al. teach some of the distinctive features between PSA from PCa patient serum, in relation to seminal plasma, could be attributed to differences in Fuc and GalNAc content. In PCa, the fucosylated structures are greatly reduced and GalNAc structures are not detectable. Tabares et al. teach in seminal plasma, GalNAc structures are clearly present. (page 133, right column, last paragraph). Tabares et al. teach a PSA glycan structure (page 136, Table 1 FcA2G1GN1). The structure taught by Tabares is the same structure recited in claim 1 (Formula 1, A)(applies to claim 6). Tabares et al. teach that the difference between PSA glycans from a prostate cancer (PCa) patient serum and PSA glycans from seminal plasma is useful for distinguishing between normal and tumor PSA. Tabares et al. teach that the amount of pure PSA needed for glycan sequencing requires large serum volumes and several purification steps, so they developed different methods to characterize and study PSA glycans from PCa patients’ sera. Glycan characterization of PSA is carried out using lectins. Tabares et al. teach that before lectin characterization, sera was treated either by immunoprecipitation or by thiophilic absorption to increase the concentration of PSA in relation to the other serum proteins present. Three immunosorbed PSA samples (from seminal plasma, from a PCa patient serum and secreted by the PCa cell line LNCaP) were compared by western blotting using lectins Sambucus nigra (SNA), Mackia amurensis (MAA), Aleuria aurantia (AAL) and Erithrina cristagalli lectin (ECL)(page 135 and Figure 4)(applies to claims 6 and 7). Tabares et al. teach the employed antibodies and lectins are labeled with a fluorescent dye. Tabares et al. teach primary and secondary capture molecules for the ligand binding assays (page 137, 3rd full paragraph and page 141, left column, 3rd paragraph-page 143)(applies to claims 10 and 12). Tabares et al. teach that lectin ECL strongly recognizes the Galβ1–4GlcNAc epitope and it is more abundant in PSA from a PCa patient serum than in PSA from seminal plasma, which presented more GalNAc in its terminal oligosaccharide structures. Tabares et al. teach that ECL detection by western blotting or ELISA, therefore, allowed PSA of PCa A serum to be distinguished from that of seminal plasma (page 140, lines 11-17 and Figure 5a)(applies to claim 9).
Tabares et al. do not teach wherein surface plasmon field-enhanced fluorescence spectroscopy is used for detection in ligand binding. Tabares et al. do not teach wherein the employed lectins are Wisteria floribunda agglutinin (WFA), soybean agglutinin (SBA), Vicia villosa lectin (VVL), or Trichosanthes japonica agglutinin (TJA-II)
Yamashita et al. teach lectin Trichosanthes japonica lectin-II (TJA-II) recognizes and binds to β-GalNAc residue on PSA (para 0045)(applies to claim 11). Yamashita et al. teach Surface Plasmon-field enhanced Fluorescence Spectroscopy (SPFS). Yamashita et al. teach that in SPFS, a measurement target is generally quantified in the mode of a sandwich assay where a ternary complex composed of an immobilization probe (antibody), the measurement target and a fluorescent-labeling probe (lectin or antibody) is formed. Yamashita et al. teach by measuring the intensity of the fluorescence emitted from the fluorescent substance and comparing the thus measured value against the intensity of fluorescence measured using a standard sample having a known concentration, the concentration of the measurement target in a blood sample can be determined. Such SPFS is extremely sensitive as compared to common fluorescent labeling methods and the like; therefore, it is capable of determining the concentration of a measurement target even when the measurement target is contained in a sample at an extremely low concentration (paras 0050 and 0054)(applies to claim 8).
It would have been obvious for one of ordinary skill in the art before the effective filling date to modify a method for quantifying PSA as taught by Tabares et al., by using lectin TJA-II and the SPFS assay, as taught by Yamashita et al. One of ordinary skill in the art before the effective filing date, would have been motivated to make such modifications and expect success for the following reasons.
Tabares et al. teach that lectin ECL strongly recognizes β-GalNAc residue on PSA from the sample of prostate cancer patients and that ECL detection by western blotting or ELISA, allows PSA of prostate cancer (PCa) serum to be distinguished from that of seminal plasma. Yamashita et al. teach SPFS is extremely sensitive as compared to common fluorescent labeling methods and is capable of determining the concentration of a target in samples at extremely low concentrations. Yamashita et al. teach that lectin TJA-II recognizes and binds to β-GalNAc residue on PSA. Using an assay, such as SPFS, would be useful when a target in a sample is at very low concentration. TJA-II provides another lectin choice that binds β-GalNAc residue on PSA.
Conclusion
No claims are allowed.
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/R.M.D/Examiner, Art Unit 1647 7/20/2026
/BRIDGET E BUNNER/Primary Examiner, Art Unit 1647
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