DETAILED ACTION
Status of Application
Claims 1-20 are pending
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s election without traverse of Group I, claims 1-10, drawn to a method of preparation for a yak hide-derived oligopeptide ferrous chelate with a high antioxidant activity, as submitted in communication filed on 06/01/2026 is acknowledged.
Claims 11-20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 06/01/2026.
Claims 1-10, are at issue and will be examined to the extent they encompass the elected invention.
Priority
Acknowledgment is made of a claim for foreign priority under 35 U.S.C. 119(a)-(d) to CHINA 202311079587.5 filed on 08/25/2023. Receipt is acknowledged of papers submitted under 35 U.S.C. 119(a)-(d), which papers have been placed of record in the file.
Drawings
The drawings submitted on 04/26/2024 have been reviewed and are accepted by
the examiner for examination purposes.
Claim Objections
Claim 4 is objected to due to the recitation of “steps: (1)….(2)…and (3)….”. Since claim numbering already uses Arabic numerals, to avoid confusion, the itemization labels should be replaced with, for example, (i), (ii) and (iii), or (a), (b) and (c). Appropriate correction is required.
Claim 4 is objected to due to the recitation of “…pretreating a yak hide: mechanically..”. It should read “…pretreating a yak hide by mechanically ..”.
Claim 4 is objected to due to the recitation of “…conducting enzymatic hydrolysis: subjecting the yak hide…”. It should read “…conducting enzymatic hydrolysis by subjecting the yak hide…”. Appropriate correction is required.
Claim 4 is objected to due to the recitation of “…conducting separation and purification by gel chromatography: subjecting the yak skin…”. It should read “…conducting separation and purification by gel chromatography by subjecting the yak skin…”. Appropriate correction is required.
Claim 4 is objected to due to the recitation of “hydrolysis using different proteases of neutral protease, alkaline protease…..and bromelain separately”. It should read “….hydrolysis using different proteases separately, wherein said proteases are selected from the group consisting of a neutral protease, an alkaline protease…and bromelain”. Appropriate correction is required.
Claim Rejections - 35 USC § 112(b) or Second Paragraph (pre-AIA )
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-10 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 1 (claims 2-10 dependent thereon) is indefinite due to the term “high antioxidant activity” for the following reason: It is a relative term which renders the claim indefinite. The term “high antioxidant activity” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree. For examination purposes, no patentable weight will be given to the term “high antioxidant activity”. Correction is required.
Claim 1 (claims 2-10 dependent thereon) is indefinite in the recitation of “with a mass concentration of the yak…oligopeptide of 1% to 5% under a pH…”, for the following reason: it is unclear which solution has to have the recited mass concentration in this case. For examination purposes, no patentable weight will be given to the term “with a mass concentration of the yak…oligopeptide of 1% to 5% under a pH…”. Correction is required.
Claim 2 (claim 7 dependent thereon) is indefinite in the recitation of “mass ratio of 2:7:1 with a mass concentration of the yak…oligopeptide of 3%”, for the following reason: The mass ratio recited has 3 numbers but it is unclear as to which are the 3 components for the recited ratio. The preamble of the claim refers to the oligopeptide and the iron source. There is no third component. Also, the recited mass concentration of 3% is unclear because one cannot determine what has to have the recited mass concentration of 3%. For examination purposes, no patentable weight will be given to the term “mass ratio of 2:7:1 with a mass concentration of the yak…oligopeptide of 3%”. Correction is required.
Claim 3 (claim 8 dependent thereon) is indefinite due to the term “relatively high iron chelating capacity” for the following reason: It is a relative term which renders the claim indefinite. The term “relatively high iron chelating capacity” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree. For examination purposes, no patentable weight will be given to the term “relatively high iron chelating capacity”. Correction is required.
Claim 4 (claim 9 dependent thereon) is indefinite in the recitation of “specifically comprising the following steps”, for the following reason: it is unclear as to how the term “specifically” further limits the claim. For examination purposes, no patentable weight will be given to the term “specifically comprising the following steps”. Correction is required.
Claim 4 (claim 9 dependent thereon) is indefinite in the recitation of “NaCl solution with a mass fraction of 5%”, for the following reason: it is unclear what the mass fraction is. For examination purposes, no patentable weight will be given to the term “mass fraction”. Correction is required.
Claim 4 (claim 9 dependent thereon) is indefinite in the recitation of “material to liquid ratio”, for the following reason: it is unclear what material and liquid is being referred to. For examination purposes, no patentable weight will be given to the term “material to liquid ratio”. Correction is required.
Claim 4 (claim 9 dependent thereon) is indefinite in the recitation of “flavor protease”, for the following reason: this term does not convey a particular structure or a specific protease activity. Therefore, it is unclear what proteases are encompassed or excluded by the term “flavor”. For examination purposes, no patentable weight will be given to the term “flavor protease”. Correction is required.
Claim 4 (claim 9 dependent thereon) is indefinite in the recitation of “an amount of the protease added at 2% of a mass of the yak hide homogenate..”, for the following reason: it is unclear how much of the protease is being added. The term “a mass of the yak hide homogenate” could be a fraction of the entire homogenate. Therefore, if the intended limitation is adding protease 2% of any fraction of the homogenate, then the protease added can be any amount because a fraction can be of any size. If the intended amount of protease is 2% of the entire mass of the yak hide homogenate, then it should be amended accordingly. Correction is required.
Claim 4 (claim 9 dependent thereon) is indefinite due to step (3) being unclear because while step (2) requires hydrolysis with a flavor protease, step (3) also requires hydrolysis with a flavor protease. Therefore, it is unclear if there are two flavor protease hydrolysis, one in step (2) and another in step (3), wherein the second flavor protease hydrolysis happens after the purification step with gel chromatography. Correction is required.
Claim 4 (claim 9 dependent thereon) is indefinite in the recitation of “(4)…with a mass concentration of 1% to 5% to obtain a mixed solution”, for the following reason: it is unclear which compound/material has to have a mass concentration of 1% to 5%. For examination purposes, no patentable weight will be given to the term “(4)…with a mass concentration of 1% to 5% to obtain a mixed solution”. Correction is required.
Claim 4 (claim 9 dependent thereon) is indefinite in the recitation of “(4)…oligopeptide and the FeS04…solution are at a mass to volume ratio of…”, for the following reason: it is unclear which compound/material is associated with “mass” and which is the compound/material associated with “volume”. It is unclear if the mass is related to the oligopeptide and if the volume is related to the iron solution. For examination purposes, no patentable weight will be given to the term “(4)…oligopeptide and the FeS04…solution are at a mass to volume ratio of…”. Correction is required.
Claim 4 (claim 9 dependent thereon) is indefinite in the recitation of “(5) adding 4 times a volume of the absolute ethanol… with a high antioxidant activity”, for the following reason: The term “a volume of the absolute ethanol” can be any volume due to the recitation of “a”. 4 times of any volume of absolute ethanol is any volume of absolute ethanol. Therefore, it is unclear as to how the term “4 times of a volume of absolute ethanol” further limits how much ethanol is added. In addition, the term “high antioxidant activity” is a relative term and the claim falls to disclose the reference required to determine the requisite degree (how much is “high” antioxidant activity?). For examination purposes, no patentable weight will be given to the term “high antioxidant activity”. For examination purposes, the term “adding 4 times a volume of the absolute ethanol…” will be interpreted as “adding absolute ethanol…”. Correction is required.
Claim Rejections - 35 USC § 103 (AIA )
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.
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.
Claims 1-4, and 6-10 are rejected under 35 U.S.C. 103 as being unpatentable over Yang et al. (Journal of Chemistry 2019.1: 9105605 published 2019; hereby “Yang”), in view of Wang et al. (International Journal of Food Science and Technology 46.8: 1705-1710. published 2011; hereby “Wang”, in further view of Wenhang Wang et al. (International Journal of Food Properties 20.5: 968-978 published 2017; hereby “Wenhang”), and as evidenced by Uniprot ID: A0A8B9WNF1_BOSMU and Genebank: ELR46121.1.
Yang teaches a method to prepare yak skin gelatin hydrolysates (YSGH) from yak skin through enzymatic hydrolysis and investigates the functional characterization of YSGH (abstract). Yang teaches that the molecular range of YSGH peptides are 400 to 3500 Da (Page 5, 3.4 Amino Acid Composition and Molecular Weight, left column). Yang teaches a pretreatment of yak skin, wherein the skin was soaked in water, and its impurities and hair were cleaned and removed, then chopped into 0.5 × 0.5 cm2 pieces and stored at − 20 °C. (Page 2. Section 2.2. Pretreatment of Yak Skin). Yang teaches a pretreatment of Yak Skin wherein fat and noncollagen proteins are removed (Page 2. Section 2.2. Pretreatment of Yak Skin). Yang teaches that the pretreated yak skin was rinsed with 0.2% HCl (w/v) solution (1:8, w/v) for 4 h at room temperature followed by rinsing with water until it reached a pH of 7.0 (Page 2, Section 2.3. Extraction of Gelatin). Yang teaches that the pretreated yak skin residues were then soaked in distilled water (85° C) until the skin was completely dissolved in the solution, and the supernatant was collected by centrifugation at 6580 ×g for 15 min at room temperature, then concentrated by rotary evaporation and lyophilized by a freeze drier (Page 2, Section 2.3. Extraction of Gelatin). Yang teaches that after the pretreatment of yak skin enzymatic hydrolysis was preformed using different proteases, which included neutrase (pH 7.0, 45 °C), pepsin (pH2.0, 37° C), trypsin (pH 7.5, 50 °C), and papain (pH 6.2, 25 ° C) (Page 2, 2.4. Enzymatic Hydrolysis). Yang teaches that the enzymatic hydrolysis resulted in hydrolysate solutions for each protease used, which was then centrifuged at 6580 ×g for 15 min (Page 2, 2.4. Enzymatic Hydrolysis). Yang teaches gel permeation chromatography on YSGH (Page 5, 3.4 Amino Acid Composition and Molecular Weight). Yang teaches the optimization of enzymatic parameters by designing experiments with different levels of variables which included: pH, temperature, E/S, substrate concentration, and hydrolysis time (Page 4, 3.3. Optimization of Enzymatic Parameters and Supplemental Table 1). Yang does not teach of an oligopeptide ferrous chelate with an iron chelating capacity or the use of glacial acetic acid.
Wang teaches that iron-chelated peptides could increase the stability, absorption and bioavailability of iron (Page 1705 [2]). Wang teaches the preparation of a yak casein hydrolysate–iron complex, wherein the hydrolysate was prepared with alcalase (Page 1706 [4]-[5]). Wang teaches of mixing yak derived hydrolysates in a FeSO4 solution to bind iron to the hydrolysates (Page 1706 [4]-[5]). Wang discloses a time course of ferrous-binding capacity of the hydrolysate, wherein ferrous-binding capacities ranged from 13.55% to 64.89% (Figure 1). Wang teaches that the degree of hydrolysis is affect the ferrous-binding activity of the hydrolysates (Page 1707, [3]-[4]). Wang discloses a mass ratio of yak hydrolysate to FeSO4 of 30:1, 15:1, 10:1, 1:1, and 1:5 (Figure 2a). Wang teaches the ferrous-binding capacity of the hydrolysate at different reaction temperatures of 20, 30, 40 and 50°C (Figure 2b), and it was shown that ferrous-binding capacity of yak casein hydrolysate increased gradually with the rising temperature (Page 1707 [6]). Wang teaches the ferrous-binding capacity of the hydrolysate at different pHs of 3.0, 4.5, 6.0, 7.5 and 9.0. pH (Figure 2c). Wang teaches the ferrous-binding capacity of the hydrolysate at different times of 10, 20, 30, 40 min (Figure 2d).
Wenhang teaches a method for preparing bovine hides by adding glacial acetic acid to the collagen to make the collagen fiber swell into a homogeneous solution, followed by a homogenization (Page 969 [5]).
Claims 1-2, 4, and 6-10 are directed in part to a preparation method of a yak hide-derived oligopeptide ferrous chelate, comprising subjecting a protein source and an iron source to chelation in water, wherein the protein source is a yak skin-derived collagen oligopeptide with a molecular weight of less than 2 kDa; and the yak skin-derived collagen oligopeptide and the iron source are subjected to the chelation in a mass ratio of 1:1 to 5:1, under a pH value of 3 to 8, specifically 6.8, at 30°C to 70°C, specifically 50°C, for 20 min to 60 min, specifically 40 min, and a corresponding prepared yak hide-derived oligopeptide ferrous chelate shows an iron chelating capacity of 42.72 mg/g±0.65 mg/g; comprising the following steps: (a) pretreating a yak hide: mechanically depilating the yak hide, removing subcutaneous muscle and fat, rinsing with water to remove surface soft flocks, cutting the yak hide into small pieces of 1 cm×1 cm, and subjecting the yak hide to defatting with a 5% Na2CO3 aqueous solution at 4°C for 18 h to obtain a defatted yak hide; adding a NaCl solution into the defatted yak hide and stirring continuously to remove salt-soluble non-collagen components, rinsing the defatted yak hide with distilled water multiple times to obtain a clean yak skin, and storing the clean yak hide at -20°C for later use; adding the clean yak skin into 0.5 mol/L glacial acetic acid to allow swelling for 12 h, and conducting homogenization using a high-speed tissue masher at 10,000 r/min to obtain a yak hide homogenate to allow subsequent enzymatic hydrolysis; (b) conducting enzymatic hydrolysis: subjecting the yak hide homogenate to enzymatic hydrolysis using different proteases like a neutral protease, alkaline protease, complex protease, papain, and bromelain separately; wherein the enzymatic hydrolysis comprises: the enzymatic hydrolysis using the alkaline protease is conducted at a pH value of 10, while the enzymatic hydrolysis using the other proteases is conducted at a pH value of 7, and the enzymatic hydrolysis is conducted at 50°C for 4 h with an amount of the protease added at 2% of a mass of the yak hide homogenate; heating a resulting enzymatic hydrolyzate at 95°C for 15 min to terminate the enzymatic hydrolysis, and then conducting centrifugation under a room temperature at 5,000 r/min for 20 min to obtain a supernatant; precipitating a polysaccharide in the supernatant using absolute ethanol, and then conducting centrifugation at 4,000 r/min for 20 min to obtain a yak skin-derived collagen peptide solution obtained by the enzymatic hydrolysis using each of the different proteases; (c) conducting separation and purification by gel chromatography: subjecting the yak skin-derived collagen peptide solution obtained by the enzymatic hydrolysis using each of the different proteases to separation and purification by gel chromatography to obtain a yak skin-derived collagen peptide; subjecting the yak skin-derived collagen peptide to enzymatic hydrolysis using the a protease under a pH value of 7 at 50°C for 4 h with an amount of the protease added to the yak skin-derived collagen peptide to obtain the yak hide-derived collagen oligopeptide; (d) mixing the yak skin-derived collagen oligopeptide and a FeSO4·7H2O solution to obtain a mixed solution, adjusting the mixed solution to a pH value of 3 to 8 with 1 mol/L NaOH or 1 mol/L HCl, and subjecting the mixed solution to the chelation at 30°C to 70°C for 20 min to 60 min; and (e) adding absolute ethanol into a resulting reaction product to precipitate a chelate of a yak hide-derived oligopeptide and ferrous ions after the chelation is completed; conducting centrifugation at 10,000 r/min for 15 min, and collecting a resulting precipitate to allow freeze-drying to obtain the yak hide-derived oligopeptide ferrous chelate; wherein the yak hide-derived oligopeptide ferrous chelate comprises 11.18%±1.08% of iron.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the method of Yang to prepare yak skin gelatin hydrolysates by incorporating the glacial acetic acid of Wenhang and further using the hydrolysates to prepare hydrolysate-iron complexes as taught in Wang. A person of ordinary skill in the art is motivated to use glacial acetic acid in methods to prepare collagen because glacial acetic acid can cause collagen to swell and aid in homogenization as taught by Wenhang, thereby facilitating collagen processing. A person of ordinary skill in the art is further motivated to use the yak skin hydrolysates of Yang to prepare iron complexes because Wang teaches that iron-chelated peptides could increase the stability, absorption and bioavailability of iron and provides a preparation method to create iron complexes. One of ordinary skill in the art has a reasonable expectation of success at arriving to modifying the method of Yang to prepare yak skin gelatin hydrolysates by incorporating the glacial acetic acid of Wenhang and further using the hydrolysates to prepare hydrolysate-iron complexes as taught in Wang because all that is required is adding glacial acetic acid to the method of Yang to prepare the yak skin then use the hydrolysate taught by Yang to prepare hydrolysate–iron complexes. Specifically, regarding the chelation in a mass ratios, mass concentrations, iron chelating capacities, centrifugation levels, reaction times, and temperatures, one of ordinary skill could optimize the methods taught above to arrive at the recited variables through routine experimentation. Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention. Additionally, MPEP section 2111.04 states “a whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited". Claim 6-11 merely states an intended result of claims 1-5, and does not include additional process steps.
Furthermore, claim 3 is directed in part to the preparation method according to claim 1, wherein the yak skin-derived collagen oligopeptide is a peptide segment and comprises SEQ ID NO: 1: GADGAPGKDGVRG and SEQ ID NO: 2: GPRGDQGPVGR. It is noted that SEQ ID NOs: 1 and 2 are known yak collagens as evidenced by having 100% sequence identity to A0A8B9WNF1_BOSMU (Uniprot) and ELR46121.1 (Genebank), respectively. See alignments below.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use known yak collagens as the collagens in the modified preparation methods of Yang and Wang. A person of ordinary skill in the art is motivated to incorporate known yak collagens in the modified preparation methods of Yang and Wang because these sequences are wild yak collagens, and Yang already employs yak collagen derived peptides. Since the evidence above establishes that SEQ ID NO: 1 and 2 are known yak collagen sequences, one of ordinary skill in the arts would have recognized the disclosed collagens as an alternate collagen source for use in a collagen preparation method. Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention.
SEQ ID NO: 1
RESULT 29
A0A8B9WNF1_BOSMU
ID A0A8B9WNF1_BOSMU Unreviewed; 1264 AA.
AC A0A8B9WNF1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Fibrillar collagen NC1 domain-containing protein {ECO:0000259|PROSITE:PS51461};
OS Bos mutus grunniens (Wild yak) (Bos grunniens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=30521 {ECO:0000313|Ensembl:ENSBGRP00000009361.1, ECO:0000313|Proteomes:UP000694520};
RN [1] {ECO:0000313|Ensembl:ENSBGRP00000009361.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang S., Liu J.;
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBGRP00000009361.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSBGRP00000009361.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
Query Match 100.0%; Score 71; Length 1264;
Best Local Similarity 100.0%;
Matches 13; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 GADGAPGKDGVRG 13
|||||||||||||
Db 470 GADGAPGKDGVRG 482
SEQ ID NO: 2
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226
776
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691
664
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Greyscale
Claim 5 is rejected under 35 U.S.C. 103 as being unpatentable over Yang et al. (Journal of Chemistry 2019.1: 9105605 published 2019; hereby “Yang”), in view of Wang et al. (International Journal of Food Science and Technology 46.8: 1705-1710. published 2011; hereby “Wang”, as applied to claim 1 above, in further view of Li et al. (Food Bioscience 41: 100991 published 2021; hereby “Li”).
Yang teaches performing the DPPH radical scavenging assay with the YSGH, wherein YSGH exhibited great antioxidant activities against DPPH, superoxide, and hydroxyl radicals, indicating that YSGH has great potential in being an antioxidant against oxidative damage (Page 7, 3.6 Biological Properties of YSGH). Yang does not teach about ABTS.
Li teaches performing ABTS and DPPH radical scavenging assays on collagen (Page 2, Section 2.3-2.4). Li teaches that collagen has high radical scavenging activity (abstract).
Claim 5 is directed in part to ahe preparation method according to claim 1, wherein a yak hide-derived oligopeptide ferrous chelate prepared by the preparation method has a better capacity in scavenging a 2,2-diphenyl-1-picrylhydrazyl (DPPH) free radical and a 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) free radical than that of a yak hide-derived oligomeric collagen peptide.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to evaluate the antioxidant activity of the iron complex prepared by Yang and Wang by preforming DPPH and ABTS radical scavenging assays as taught by Li. A person of ordinary skill in the art is motivated to perform DPPH and ABTS radical scavenging assays because Li teaches DPPH and ABTS radical scavenging assays are routine experiments used for evaluating the antioxidant activity of collagen, and Yang already preformed the DPPH radical scavenging assay and has shown that YSGH has improved radical scavenging of DPPH. One of ordinary skill in the art has a reasonable expectation of success at arriving to employing the radical scavenging of DPPH and ABTS taught by Li to further characterize collagen because all that is required is performing established techniques for assessing collagen. Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention. Additionally, MPEP section 2111.04 states “a whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited". Claim 5 merely states an intended result of claim 1, and does not include additional process steps.
Conclusion
No claim is in condition for allowance.
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/S.L.S./Examiner, Art Unit 1652
/ROBERT B MONDESI/Supervisory Patent Examiner, Art Unit 1652
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