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 Claims
Claims 1, 4, 6, 7, 9-18 and 20 are currently pending. Claims 1, 4, 9, 17 and 18 have been amended by Applicants’ amendment filed 11-07-2025. Claims 3 and 19 have been canceled by Applicants’ amendment filed 11-07-2025. No claims have been added by Applicants’ amendment filed 11-07-2025.
Applicant's election of Group I, claims 1-10 and 12, directed to a protein-binding product; and a device containing said protein-binding product according to claim 1, in the reply filed October 18, 2023 was previously acknowledged.
Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election of invention has been treated as an election without traverse (MPEP
§ 818.03(a)).
Claims 11 and 13-16 were previously withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a non-elected species, there being no allowable generic or linking claim.
The restriction requirement was deemed proper and was made FINAL.
A complete reply to the final rejection must include cancellation of nonelected claims or other appropriate action (37 CFR 1.144) See MPEP § 821.01.
Therefore, claims 1, 4, 6, 7, 9, 10, 12, 17, 18 and 20 are under consideration to which the following grounds of rejection are applicable.
Priority
The present application filed September 8, 2020 is a 35 U.S.C. 371 national stage filing of International Application No. PCT/SE2019/050211, filed on March 8, 2019, which claims the benefit of Swedish Patent Application SE1800056-2, filed March 8, 2018.
Withdrawn Objections/Rejections
Applicants’ amendment and arguments filed November 7, 2025 are acknowledged and have been fully considered. The Examiner has re-weighed all the evidence of record. Any rejection and/or objection not specifically addressed below are herein withdrawn.
Claim Rejections - 35 USC § 112(a) – New Matter
The rejection of claims 1, 4, 6, 7, 9, 10, 12, 17, 18 and 20 is withdrawn under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement.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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention due to Applicant’s amendment of the claims, in the reply filed 11-07-2025.
In view of the withdrawn rejection, Applicant’s arguments are rendered moot.
Maintained Objections/Rejections
Claim Rejections - 35 USC § 112(b)
The rejection of claims 1, 4, 6, 7, 9, 10, 12, 17, 18 and 20 is maintained under 35 U.S.C 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention.
The rejection of claims 1 and 12 is maintained as being indefinite for the recitation of the term “the derivative” in claim 1, line 7. There is insufficient antecedent basis for the term “the derivative” in the claim because claim 1, line 6 recites the term “a disaccharide derivative.” The Examiner suggests that Applicant amend the claim to recite, for example, “the disaccharide derivative.”
The rejection of claims 1 and 12 is maintained as being indefinite for the recitation of the term
“3-OR2 group” in claim 1, lines 12-14 and 19 because it is unclear whether the R2 derivative group of “3-OR2 group” is related to the spacer (R) recited in claim 1, line 4. No spacer R is shown in any structure, illustration, and/or formula in claim 1, such that its reason for inclusion is unclear and, thus, the metes and bounds of the claim cannot be determined.
Claims 1 and 12 are indefinite for the recitation of the term “when said disaccharide ligand is a Gab1-4GlcNAcb-O- derivative, the substituent is one of groups a)-(d), but not for b) when R2 group is a D-galactosyl group” such as recited in claim 1, lines 18-20 because it is unclear what substituents are excluded from the derivative, and under what circumstances the substituent is excluded. It is unclear whether the substituent is one of (a)-(d) as recited; whether the substituent is one of (a), (c) and (d); or whether some other substituents for the Gab1-4GlcNAcb-O- ligand are provided or excluded and, thus, the metes and bounds of the claim cannot be determined.
The rejection of claims 6, 7 and 18 is maintained as being indefinite for the recitation of the term “per mL polymer” such as recited in claim 6, line 2 because claim 6 depends from instant claim 1, wherein claim 1 does not does not recite a method of making the porous polymer bead, the presence of a polymer solution, any ratio of disaccharide ligand to polymer solution, and/or that the polymer solution is a porous polymer solution and, thus, the metes and bounds of the claim cannot be determined.
Claims 4, 9, 10, 17 and 20 are indefinite insofar as they ultimately depend from instant claim 1.
Response to Arguments
Applicant’s remarks filed November 7, 2025 have been fully considered but they are not persuasive. Applicants essentially assert that: (a) regarding claims 1, 12 and 17 including the terms “the derivative,” proper antecedent basis has been provided (Applicant Remarks, pg. 6, last partial paragraph through pg. 7, first partial paragraph); and (b) regarding the term per mL polymer, the polymer is present in the porous polymer beads (Applicant Remarks, pg. 7, first partial paragraph).
Regarding (a), proper antecedent basis is not found for the term “the derivative.” Thus, the claims remains rejected.
Regarding (b), regarding the term “per mL polymer,” it is noted that instant claims 6, 7 and 18 depend from claim 1, where claim 1 does not recite a method of making the porous polymer bead, the presence of a polymer solution, any ratio of disaccharide ligand to polymer solution, and/or that the polymer solution is a porous polymer solution. The claims remain rejected.
Claim Rejections - 35 USC § 102
The rejection of claims 1, 6, 7, 9, 10, 12, 17, 18 and 20 is maintained under 35 U.S.C. 102(a1)/102(a2) as being anticipated by Nilsson et. al. (hereinafter “Nilsson”) (US Patent Application Publication No. 20040022784, published February 5, 2004; of record) as evidenced by Nilsson et. al. (hereinafter “Nilsson ‘230”) (US Patent Application Publication No. 2020406230, published December 31, 2020).
Regarding claims 1, 17 and 20, Nilsson teaches material characterized by that the material contains at least one biologically active saccharide which is covalently bound via at least one spacer to a cross-linked matrix and that the material is autoclaved (interpreted as a disaccharide covalently bound; and a spacer, claim 1) (Abstract). Nilsson teaches that a saccharide can consist of a glycoprotein, a neoglycoprotein, a glycopeptide or a glycosylated amino acid, a glycolipid, or a part, a fragment or a modified variant thereof, or another biologically active disaccharide or trisaccharide or higher oligosaccharide substance (interpreted as a disaccharide, claim 1) (paragraph [0005]). Nilsson teaches that the material consists, as a non-limiting example, of for example either: Blood group A-O(CH2)n-PhNH-CO(CH2)mNH-CH2-CH(OH)-CH2-O-Matrix or: Blood group B-O(CH2)nPhNH-CO-(CH2)mNH-CH2-CH(OH)-CH2-O-Matix, wherein “Matrix” denotes a plastic or a polysaccharide, such as a cross-linked agarose or Sepharose Fast Flow; -O(CH2)n-PhNH-CO(CH2)mNH-CH2-CH(OH)-CH2-O- is a spacer; n is an integer from 0 to 4; and m is an integer from 0 to 7 (interpreted as a aliphatic and/or aromatic spacer; and bloods groups A and B (interpreted as bound to a matrix that binds a blood group A specific antibody, and blood group B-specific antibody; and porous polymer beads, claims 1 and 17) (paragraphs [0008]-[0011]). Nilsson teaches that instead of the -O(CH2)2PhNH- group in the formulas supra, another suitable Spacer or part of Spacer can be used including -O-(CH2)nNH- or another aliphatic compound, or another aromatic compound (interpreted as an aliphatic or aromatic spacer; and the spacers recited in claim 9, claims 1 and 9) (paragraph [0021]). Nilsson teaches that the saccharide, for example the blood group A- or B-determinant, can also be bound, directly or indirectly, to an oligomeric substance acting as spacer, or part of spacer, as for example a monosaccharide, disaccharide, or higher oligosaccharide or polysaccharide, peptide, for example a peptide consisting of amide bound glycine and glutamic acid residues, for example Gly-(Glu-Gly)n-Glu, where n is an integer between for example 1 and 20, wherein the saccharide-spacer consists of 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 or more saccharide units bound to each oligomeric substance or peptide (interpreted as encompassing disaccharides; and carbohydrates, carbohydrate derivatives compounds or ligands that bind to blood group A or B specific antibodies, claims 1 and 17) (paragraph [0022]). Nilsson teach that an advantage of using oligomeric ligands is that antibodies towards blood group determinant or other proteins, viruses or cells can be separated to obtain a more efficient product compared with non-oligomeric ligand (interpreted as ligands that bind to blood group A or B specific antibodies; and A or B antigen, claims 1, 17 and 20) (paragraph [0026]). Nilsson teaches an aliphatic or aromatic spacer be used to bind the saccharide to the lysine residues of the peptide, but in this case is, for example, glycosidically bound groups of the type -O(CH2)2PhCOO-, or for example O(CH2)nCOO-, used for carbodiimide- or succinimide-mediated coupling between saccharide and lysine residues in the peptide (interpreted as aliphatic and aromatic spacers, claim 1) (paragraph [0030]). Nilsson teaches that the saccharide can then first be coupled to the protein, or to the polysaccharide, which then is coupled to the Matrix (interpreted as polymer beads that bind galactose-binding proteins, claim 1) (paragraph [0032]). Nilsson teaches that the products can be used for specific removal of proteins in connection with blood plasma separation, for example antibodies directed towards Gala1-3Gal and other so called xeno antigens in connection with xeno-transplantation (interpreted as binding human blood plasma toxins, claim 19) (paragraph [0034]). Nilsson teaches that the product according to the invention can be used with commercially available activated matrix such as NHS-activated Sepharose 4 Fast Flow, which is present in the form of practically spherical particles (interpreted as porous polymer beads comprising the disaccharide ligands of the invention as beads that bind galectins, claims 1, 4 and 12) (paragraph [0038], lines 1-7), where it is known that galectins are a class of proteins that bind specifically to b-galactoside sugars; and that the compounds of the invention can be used to quantitatively reduce the level of galectin including galectin-1, galectin-3 and galectin-8 in human blood plasma as evidenced by Nilsson ‘230 (paragraph [0002]; [0034]; and [0036], lines 1-3). Nilsson teaches Gala1-3Galb1-4GlcNAcb-; (Gala1-3Galb1-4GlcNAcb-)n-; (Gala1-3Galb1-4GlcNAcb-spacer)n- and Gal ≠ 1-3Galb1-4GlcNAcb-spacer)n-, wherein n is an integer larger than 1 (interpreted as polymer beads comprising a disaccharide ligand including Galb1-4GlcNAcb-O- and Galb1-3GlcNAcb-O- wherein R2 is a D-galactosyl (Gala) group attached at the 3-OH group of Gal; bound to a spacer; and to the surface of at least one porous polymer bead, claim 1) (paragraphs [0043]-[0044]). Nilsson teaches that other carbohydrate structures active towards other antibodies such as antibodies against cancer-antigens including breast-, prostate-, intestine-, or skin cancer can be used to form Product according to the invention (interpreted as other carbohydrate structures that bind to antibodies including receptor antibodies; interpreting cancer as a human blood plasma toxin; and A or B antigen, claims 1, 17 and 20) (paragraph [0045]).
Regarding claim 4, Nilsson teaches that the product according to the invention can be used with commercially available activated matrix such as NHS-activated Sepharose 4 Fast Flow, which is present in the form of practically spherical particles (interpreted as porous polymer beads comprising the disaccharide ligands of the invention as beads that bind galectins, claims 1, 4 and 12), where it is known that galectins are a class of proteins that bind specifically to b-galactoside sugars; and that the compounds of the invention can be used to quantitatively reduce the level of galectin including galectin-1, galectin-3 and galectin-8 in human blood plasma as evidenced by Nilsson ‘230 (paragraph [0002]; [0034]; and [0036], lines 1-3).
Regarding claims 6, 7 and 12, Nilsson teaches that the product according to the invention can be used with commercially available activated matrix such as NHS-activated Sepharose 4 Fast Flow, which is present in the form of practically spherical particles (interpreted as porous polymer beads comprising the disaccharide ligands of the invention, claims 1, 4 and 12) (paragraph [0038], lines 1-7). Nilsson teaches that the product according to the invention can use so-called epoxyactivated SepharoseR 4 Fast Flow, to which is covalently bound, for example Blood group A-O(CH2)nPhNH-CO(CH2)mNH-, or to which is covalently bound Blood group B--O(CH2)nPhNH-CO--(CH2)mNH- (interpreted as porous polymer beads comprising the disaccharide ligands of the invention, claims 1, 4 and 12) (paragraph [0039]). Nilsson teaches a single passage of more than one liter blood group B plasma with a flow rate of about 40 ml/minute through a column with about 3 micromole of blood group A trisaccharide per ml Sepharose 4 FF, wherein a total product volume of 62 ml and a particle size of 90 microns practically eliminated all antibodies reactive against blood group A and blood group B (interpreted as a column containing the binding product of claim 1; and 3 mm saccharide per ml polymer, claims 6, 7 and 12) (paragraph [0047], lines 6-13).
Regarding claim 9, Nilsson teaches that instead of the -O(CH2)2PhNH- group in the formulas supra, another suitable Spacer or part of Spacer can be used including -O-(CH2)nNH- or another aliphatic compound, or another aromatic compound (interpreted as an aliphatic or aromatic spacer; and the spacers recited in claim 9, claims 1 and 9) (paragraph [0021]). Nilsson teaches that the activated Matrix can be used for covalent binding of Blood group A-O (CH2)nPhNH2- to give product 1a, and Blood group B--(CH2)nPhNH2- to give product 2b (interpreted as a spacer of claim 9, claim 9) (paragraph [0038], lines 8-12).
Regarding claim 10, Nilsson teaches that the Matrix denotes a plastic or a polysaccharide, for example cross-linked agarose, specifically of the type Sepharose Fast Flow (interpreted as agarose and cross-linked agarose beads, claim 10) (paragraph [0010]).
Regarding claim 18, Nilsson teaches that the saccharide-spacer can be added to the reaction mixture in a desired molar excess in relation to the amount of moles of peptide, wherein the molar excess can be 2, 3, 4, 5, 6, 7, 8, 9, or 10 times excess or more; and other reaction conditions are chosen by the expert and do not limit the scope of the invention, wherein Saccharide is 0.01, 0.1, 1, 2, 3, 4, 5, 10, 15, 20 mmole of ligand per liter of matrix (interpreted as encompassing 5-20 mm per ml of polymer, claim 10) (paragraph [0024], lines 9-19).
Nilsson meets all the limitations of the claims and, therefore, anticipates the claimed invention.
Response to Arguments
Applicant’s remarks filed November 7, 2025 have been fully considered but they are not persuasive. Applicants essentially assert that: (a) Nilsson does not teach porous polymer beads that bind
galectin as previously recited in claim 3 (Applicant Remarks, pg. 8, fifth full paragraph).
Regarding (a), although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26USPQ2d 1057 (Fed. Cir. 1993). Moreover, as noted in MPEP 2112.01(I),
where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). "When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990).
Applicant’s assertion that Nilsson does not teach porous polymer beads that bind galectin as previously recited in claim 3, is not found persuasive. As an initial matter, instant claim 1 does not recite that the porous polymer beads are, in fact, bound to galectin. The instant published Specification teaches that galectins are a class of proteins that bind specifically to b-galactoside sugars (See; paragraph [0002]). Nilsson teaches materials that bind proteins, and b-galactoside sugars bound to particles including Gala1-3Galb1-4GlcNAcb-; (Gala1-3Galb1-4GlcNAcb-)n-; (Gala1-3Galb1-4GlcNAcb-spacer)n-, such that the saccharides bound to polymer particles as taught by Nilsson clearly bind galectins. Additionally, the instant published Specification teaches that the porous polymer beads comprising disaccharide ligands bound via a spacer as recited in instant claim 1 will bind galectins including galectin-1, galectin-3 and galectin-8 (See; paragraphs [0028]; [0034] and [0036]). Because Nilsson teaches all of the limitations of instant claim 1, the polymer particles of Nilsson bind galectins. Thus, the claims remain rejected.
Claim Rejections - 35 USC § 103
The rejection of claims 1, 6, 7, 9, 10, 12, 17, 18 and 20 is maintained under 35 U.S.C. 103 as being unpatentable over Nilsson et. al. (hereinafter “Nilsson”) (US Patent Application Publication No. 20040022784, published February 5, 2004; of record) in view of Iwaki et al. (hereinafter “Iwaki”) (Trends in Glycoscience and Glycotechnology, 2018, 30(172), SE137-SE153; and Supplementary Material, 2018, 30(172), 1-7; of record) as evidenced by Nilsson et. al. (hereinafter “Nilsson ‘230”) (US Patent Application Publication No. 20200406230, published December 31, 2020).
The teachings of Nilsson as applied to claims 1, 6, 7, 9, 10, 12, 17, 18 and 20 are described supra.
Nilsson does not specifically teach the term galectin (claim 4, in part).
Regarding claim 4 (in part), Iwaki teaches in Figure 1, a diagram of the Fontal Affinity Chromatograph (FAC) apparatus is shown, wherein the advantages of FAC-FD are summarized in Table 2 including wherein FAC analysis accurate concentration of analyte is not necessarily known if it is negligibly small compared to Kd; and that current FAC using PA oligo-saccharides has a few drawbacks, wherein reduced terminal monosaccharides take an open structure as a result of monoamine coupling (Figure 2), such that this is common to other methods using the same chemical procedure, e.g., 2-AA, 2-AB, ethyl p-aminobenzoate, 2-aminoacridone, and 8-aminopyrene-1,3,6-trisulfonic acid; as well as, the necessity to immobilize ligands (lectins), which can modify or reduce lectin functions, where some lectins are inactivated upon immobilization (pg. 140, col 2, first full paragraph, and last partial paragraph). Iwaki teaches that the features of galectin specificity has been demonstrated by preceding works by a Hakon Leffler's group, where they found the basic galectin-binding "epitopes" on disaccharides; and demonstrated what additions prevent binding and what additions enhance binding for some galectins, wherein these epitopes consist of three hydroxyl groups of the recognition disaccharides like lactose (Galb1-4Glc) and LacNAc (Galb1-4GlcNAc); namely C4-OH and C6-OH of non-reducing terminal Gal and C3-OH of reducing terminal Glc/GlcNAc; as well as, finding that Galb1-3Glc can be a ligand for galectins, though the affinity is considerably lower when compared with its isomer, LacNAc both in galectin-1 and galectin-3 (interpreted as lactose, LacNAc, and Galb1-3Glc as being able to bind galectins, claims 3and 4) (pg. 142, col 1, first partial paragraph). Iwaki teaches in Figure 2, a reaction scheme of monoamine coupling between a reducing sugar and a coupling agent, wherein after the coupling reaction, the derived Schiff base is reacted with NaBH2CN to stabilize the chemical structure (interpreted as a derivative, claim 1) (pg.142, Figure 2). Figure 2 is shown below:
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Iwaki teaches that based on the configuration of the glycosidic linkages regarding the reducing terminal monosaccharides are further categorized into two cases of configuration pattern: one is the "typical'' pattern comprising Galb1-4Glc (lactose), Galb1-4GlcNAc (LacNAc), GalNAcb1-4GlcNAc (LeadiNAc), GalNAcb1-4GlcA (chondroitin component), Galb1-4Man (Leishmania epitope), and Galb1-3GlcNAc (lacto-N-biose), where the equatorial 3-OH or 4-OH of the reducing terminal mono-saccharides form a hydrogen bond network with the commonly conserved Glu and Arg residues located on S6 (interpreted as the products of claim 1 that bind galectins, claims 1, 3 and 4) (pg. 142, col 2; last partial paragraph, lines 7-16). Iwaki teaches that the other configuration is the ''atypical” pattern comprising GalNAcb 1-3Gal (non-reducing terminal disaccharide in globotetraose, Gb4) and Galb1-3GalNAc (T antigen and non-reducing terminal disaccharide, GA1 ), wherein these disaccharides have been reported as galectin ligands, while the affinities for the isolated glycans were relatively low in comparison with LacNAc, where galectin-1 and galectin-3 can bind to Galb1-3GalNAc (interpreted as the products of claim 1 that bind galectins, claims 1, 3 and 4) (pg. 142, col 2; last partial paragraph, lines 16-18; and pg. 145, col 1; first partial paragraph, lines 1-4). Iwaki teaches that a variety of galectin binding to 3’-modified b-galactosides is described, wherein most galectins accommodate substitutions at this position some of them showing an enhanced affinity to the resultant saccharides unlike other galactose-binding lectins, such as R-type lectins, legume lectins, and C-type lectins, which require 3-OH group of Gal for recognition (interpreted as 3-OH group of Gal for galectin recognition, claims 1, 3 and 4) (pg. 145, col 2, first full paragraph). Iwaki teaches that chondroitin/dermatan sulfate composed of GalNAcb1-4GlcA/IdoA, selectively interacts with galectin-3, 7, 9N, and 9C (interpreted as binding galectins, claims 3 and 4) (pg. 148, col 1; last full paragraph, lines 5-6). Iwaki teaches that the two patterns (typical and atypical) are common in that the non-reducing terminal galactose is linked to a penultimate residue with a glycosidic bond to an equatorial hydroxyl group such as C3/4-OH of Glc(NAc)/GlcA/Man in typical and C3-OH of Gal(NAc) in atypical cases (pg. 145, col 1; first partial paragraph, lines 18-22). Iwaki teaches that thus far, only short O-linked glycans are available as four p-nitrophenyl derivatives of which three showed significant binding to galectins, while core 6 did not because it is not compatible with the Galb-equatorial manner (interpreted as 3-OR2 group, where R2 is an aromatic group; and binding to galectins, claims 1, 3 and 4) (pg. 150, col 1; first partial paragraph, lines 1-3). Iwaki teaches the development of galectin inhibitors, wherein T-cell activation is exquisitely modulated by tight association of galectin-3 with branched and extended N-glycans on T-cell receptor complex, wherein galectin-3 regulates plasma cell differentiation from peritoneal B1 cells, and regulates the acceleration of cancer malignancy; while galectin-1 promotes plasma cell differentiation from activated mature B cells and immunoglobulin production; and galectin-8 specifically binds to CD44 and is mediated by specific glycan recognition, while inhibition causes activation of inflammatory cells, resulting in inhibition of apoptosis of autoimmune inflammation in rheumatoid arthritis (pg 150, col 1, last partial paragraph; and col 2, first partial paragraph).
It is prima facie obvious to combine prior art elements according to known methods to yield predictable results; the court held that, "…a conclusion that a claim would have been obvious is that all the claimed elements were known in the prior art and one skilled in the art could have combined the elements as claimed by known methods with no change in their respective functions, and the combination would have yielded nothing more than predictable results to one of ordinary skill in the art. KSR International Co. v. Teleflex Inc., 550 U.S. ___, ___, 82 USPQ2d 1385, 1395 (2007); Sakraida v. AG Pro, Inc., 425 U.S. 273, 282, 189 USPQ 449, 453 (1976); Anderson’s-Black Rock, Inc. v. Pavement Salvage Co., 396 U.S. 57, 62-63, 163 USPQ 673, 675 (1969); Great Atlantic & P. Tea Co. v. Supermarket Equipment Corp., 340 U.S. 147, 152, 87 USPQ 303, 306 (1950)”. Therefore, in view of the benefits of analyzing lectin-glycan interactions as exemplified by Iwaki, it would have been prima facia obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the method of characterizing biologically active saccharides by covalently binding saccharides including Gala1-3Galb1-4GlcNAcb and Gala1-3Galb1-4GlcNAcb to at least one spacer, which binds a cross-linked matrix as disclosed by Nilsson to include different saccharide modifications such as on Galb1-4Glc, Galb1-4GlcNAc, GalNAcb1-4GlcNAc, GalNAcb1-4GlcA, Galb1-4Man, and Galb1-3GlcNAc including at equatorial Gal 3-OH or 4-OH as taught by Iwaki, with a reasonable expectation of success in evaluating modified and/or substituted di-saccharides and/or tri-saccharides for selective galectin binding activity, galectin inhibition and/or for antibody binding properties including for the removal of specific antibodies or proteins from blood, for blood-plasma separation, and/or for the treatment of disease such as cancer and immunological disorders.
Thus, in view of the foregoing, the claimed invention, as a whole, would have been obvious to one of ordinary skill in the art at the time the invention was made. Therefore, the claims are properly rejected under 35 USC §103 as obvious over the art.
Response to Arguments
Applicant’s remarks filed November 7, 2025 have been fully considered but they are not persuasive. Applicants essentially assert that: (a) paragraph [0038] of the specification reports surprising results, such that when the column contains a polymer-spacer-ligand complex, i. e. a protein--binding product, according to the present invention, e. g. a disaccharide derivative in which the 3-OH group of Gal in any of the disaccharide structures disclosed above is substituted with a 3-CO-R2 group or a 3-O-R2 group as described above, a higher reduction of the level of galectin per treated patient blood plasma volume can be achieved, such guidance to lead one to the reported results is missing from Iwaki (Applicant Remarks, pg. 9, third through sixth full paragraphs).
Regarding (a), please see the discussion supra regarding the Examiner’s response to Applicant’s arguments. It is noted that none of the references has to teach each and every claim limitation. If they did, this would have been anticipation and not an obviousness-type rejection. One cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). MPEP 2145 also states:
Rebuttal evidence may also include evidence that the claimed invention yields unexpectedly improved properties or properties not present in the prior art. Rebuttal evidence may consist of a showing that the claimed compound possesses unexpected properties. Dillon, 919 F.2d at 692-93, 16 USPQ2d at 1901. A showing of unexpected results must be based on evidence, not argument or speculation. In re Mayne, 104 F.3d 1339, 1343-44, 41 USPQ2d 1451, 1455-56 (Fed. Cir. 1997) (underline and italics added).
Additionally, the evidence must be reasonably commensurate in scope with the claimed invention. See, e.g., In re Kulling, 897 F.2d 1147, 1149, 14 USPQ2d 1056, 1058 (Fed. Cir. 1990); In re Grasselli, 713 F.2d 731, 743, 218 USPQ 769, 777 (Fed. Cir. 1983) (underline and italics added).
in order for evidence of secondary considerations to be accorded substantial weight, there must be a nexus, i.e., a legally and factually sufficient connection or correspondence between the submitted evidence and the claimed invention. Fox Factory, Inc. v. SRAM, LLC, 944 F.3d 1366, 1373, 2019 USPQ2d 483355 (Fed. Cir. 2019), cert. denied, 141 S.Ct. 373 (2020). See MPEP § 716.01(b) (underline and italics added).
MPEP 2112.01(II) indicates:
"Products of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Id. (underline added).
As an initial matter, instant claims 1 and 12 are directed to a product/device. Instant claims 1 and 12 are not directed to a method of using the device, such that Iwaki is not required to provide guidance on the use of the product/device including achieving higher reduction of the level of galectin per treated patient blood plasma. Applicant has not:
Provided evidence supporting the unexpected results asserted by Applicant.
Determined the specific reduction in the quantity of galectin that constitutes a ‘higher reduction’ in the molar quantity a patient’s blood.
Applicant’s has not provided any evidence of improved properties that are reasonably commensurate in scope with the claimed invention
Instant claims 1 and 12 do not recite: a column containing the specific polymer-spacer-ligand complex substituted 3-NH-CO-R2 group or 3-O-R2 group, and having a specific quantity of derivative; the amount of polymer used; passing blood plasma through the column; binding galectins to the porous polymer beads; assessing the binding a level of galectin per volume of treated patient blood plasma, determining a reduction in the level of galectin, comparing the reduction to some other polymer-spacer-ligand complex, etc.
There is no nexus or co-extensiveness between Applicant’s asserted improvements and the steps as recited in claims 1 and 12 including using polymer-spacer-ligand complex comprising disaccharide structures substituted with 3-NH-CO-R2 group or with a 3-O-R2 group to treat patient blood plasma.
Evidence has not been provided that the "superior results" asserted by Applicant were unknown in the prior art.
Additionally, MPEP 2112.01(II) states that products of identical chemical composition cannot have mutually exclusive properties. Because Nilsson teaches all of the limitations of claims 1 and 12, the product of Nilsson will inherently provide the same surprising benefits as asserted by Applicant. Thus, the claims remain rejected.
Conclusion
Claims 1, 4, 6, 7, 9, 10, 12, 17, 18 and 20 are rejected.
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to AMY M BUNKER whose telephone number is (313) 446-4833. The examiner can normally be reached on Monday-Friday (6am-2:30pm).
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/AMY M BUNKER/Primary Examiner, Art Unit 1684