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liquid chromatography mass spectrometry lc ms  (YMC America)
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YMC America liquid chromatography mass spectrometry lc ms
Reaction schemes <t>and</t> <t>LC-MS</t> analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.
Liquid Chromatography Mass Spectrometry Lc Ms, supplied by YMC America, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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jasco extrema lc 4000  (JASCO Inc)
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JASCO Inc jasco extrema lc 4000
Reaction schemes <t>and</t> <t>LC-MS</t> analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.
Jasco Extrema Lc 4000, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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magna pure lc automated extraction system  (Roche)
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Roche magna pure lc automated extraction system
Reaction schemes <t>and</t> <t>LC-MS</t> analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.
Magna Pure Lc Automated Extraction System, supplied by Roche, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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liquid chromatography-tandem mass-spectrometry (lc-ms/ms  (Thermo Fisher)
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Reaction schemes <t>and</t> <t>LC-MS</t> analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.
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lc grade acetonitrile  (Fisher Scientific)
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Reaction schemes <t>and</t> <t>LC-MS</t> analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.
Lc Grade Acetonitrile, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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lc 4000 uhplc 310  (JASCO Inc)
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JASCO Inc lc 4000 uhplc 310
Reaction schemes <t>and</t> <t>LC-MS</t> analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.
Lc 4000 Uhplc 310, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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jasco x lc hplc system  (JASCO Inc)
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JASCO Inc jasco x lc hplc system
Reaction schemes <t>and</t> <t>LC-MS</t> analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.
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lc 4000 hplc system  (JASCO Inc)
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JASCO Inc lc 4000 hplc system
Reaction schemes <t>and</t> <t>LC-MS</t> analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.
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jasco hplc lc net ii  (JASCO Inc)
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(A) Volcano plot of untargeted metabolomic changes in PAH enu2 brains relative to WT, showing increased Phe-related metabolites and decreased metabolites associated with tyrosine metabolism, redox balance, and central carbon metabolism. (B) Volcano plot of label-free proteomic changes in PKU brains relative to WT, highlighting significant alterations in proteins related to proteostasis, translation, neuronal signaling, and stress adaptive responses. (C) Z-score matrix showing pathway-level activity. Metabolomic and proteomic contributions are presented separately, highlighting specific alterations in redox and detoxification, proteostasis, the TCA cycle, and lipid-related pathways. (D) Integrated cell-fate matrix combining metabolomic and proteomic evidence into a single activity state. The Phe axis was the most strongly activated integrated module, whereas myelin glial remodeling was suppressed. Redox oxidative stress showed a mixed integrated pattern, consistent with pathway remodeling rather than uniform activation or suppression. (E) <t>HPLC</t> quantification of reduced glutathione (GSH), cysteine (CYS), and ATP levels in WT and PKU brain tissue. Data are expressed as mean ± SD normalized to mg of cortex (* < 0.05) (n=6/group).
Jasco Hplc Lc Net Ii, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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jasco hplc  (JASCO Inc)
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(A) Volcano plot of untargeted metabolomic changes in PAH enu2 brains relative to WT, showing increased Phe-related metabolites and decreased metabolites associated with tyrosine metabolism, redox balance, and central carbon metabolism. (B) Volcano plot of label-free proteomic changes in PKU brains relative to WT, highlighting significant alterations in proteins related to proteostasis, translation, neuronal signaling, and stress adaptive responses. (C) Z-score matrix showing pathway-level activity. Metabolomic and proteomic contributions are presented separately, highlighting specific alterations in redox and detoxification, proteostasis, the TCA cycle, and lipid-related pathways. (D) Integrated cell-fate matrix combining metabolomic and proteomic evidence into a single activity state. The Phe axis was the most strongly activated integrated module, whereas myelin glial remodeling was suppressed. Redox oxidative stress showed a mixed integrated pattern, consistent with pathway remodeling rather than uniform activation or suppression. (E) <t>HPLC</t> quantification of reduced glutathione (GSH), cysteine (CYS), and ATP levels in WT and PKU brain tissue. Data are expressed as mean ± SD normalized to mg of cortex (* < 0.05) (n=6/group).
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Reaction schemes and LC-MS analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.

Journal: Synthetic and Systems Biotechnology

Article Title: Functional characterization of four glycosyltransferases for biosynthesis of steroidal saponins in medicinal plant Paris polyphylla

doi: 10.1016/j.synbio.2026.04.002

Figure Lengend Snippet: Reaction schemes and LC-MS analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.

Article Snippet: Liquid chromatography-mass spectrometry (LC-MS) was equipped with a YMC-Triart C18 column (250 mm × 4.6 mm, 5 μm), and the column temperature was set to 30 °C.

Techniques: Liquid Chromatography with Mass Spectroscopy, Transferring, In Vitro, Activity Assay, Recombinant, Control, Expressing, Plasmid Preparation, Tandem Mass Spectroscopy

(A) Volcano plot of untargeted metabolomic changes in PAH enu2 brains relative to WT, showing increased Phe-related metabolites and decreased metabolites associated with tyrosine metabolism, redox balance, and central carbon metabolism. (B) Volcano plot of label-free proteomic changes in PKU brains relative to WT, highlighting significant alterations in proteins related to proteostasis, translation, neuronal signaling, and stress adaptive responses. (C) Z-score matrix showing pathway-level activity. Metabolomic and proteomic contributions are presented separately, highlighting specific alterations in redox and detoxification, proteostasis, the TCA cycle, and lipid-related pathways. (D) Integrated cell-fate matrix combining metabolomic and proteomic evidence into a single activity state. The Phe axis was the most strongly activated integrated module, whereas myelin glial remodeling was suppressed. Redox oxidative stress showed a mixed integrated pattern, consistent with pathway remodeling rather than uniform activation or suppression. (E) HPLC quantification of reduced glutathione (GSH), cysteine (CYS), and ATP levels in WT and PKU brain tissue. Data are expressed as mean ± SD normalized to mg of cortex (* < 0.05) (n=6/group).

Journal: bioRxiv

Article Title: Integrated metabolic and proteostatic profiling reveals remodeling of proteolytic pathways associated with redox-bioenergetic dysfunction in a PAH enu2 mouse model of phenylketonuria

doi: 10.64898/2026.07.08.736353

Figure Lengend Snippet: (A) Volcano plot of untargeted metabolomic changes in PAH enu2 brains relative to WT, showing increased Phe-related metabolites and decreased metabolites associated with tyrosine metabolism, redox balance, and central carbon metabolism. (B) Volcano plot of label-free proteomic changes in PKU brains relative to WT, highlighting significant alterations in proteins related to proteostasis, translation, neuronal signaling, and stress adaptive responses. (C) Z-score matrix showing pathway-level activity. Metabolomic and proteomic contributions are presented separately, highlighting specific alterations in redox and detoxification, proteostasis, the TCA cycle, and lipid-related pathways. (D) Integrated cell-fate matrix combining metabolomic and proteomic evidence into a single activity state. The Phe axis was the most strongly activated integrated module, whereas myelin glial remodeling was suppressed. Redox oxidative stress showed a mixed integrated pattern, consistent with pathway remodeling rather than uniform activation or suppression. (E) HPLC quantification of reduced glutathione (GSH), cysteine (CYS), and ATP levels in WT and PKU brain tissue. Data are expressed as mean ± SD normalized to mg of cortex (* < 0.05) (n=6/group).

Article Snippet: Detection was performed at 254 nm using a Jasco HPLC LC-net II (Jasco Inc., Japan).

Techniques: Metabolomic, Activity Assay, Activation Assay

HPLC quantification of (A) ATP, ADP, AMP, NAD, and NADH levels from WT and PKU mice; (B) reduced glutathione (GSH) and cysteine contents in whole blood (n=6/group). (C) Activities of glutathione peroxidase (GPX), glutathione reductase (GR), and glucose-6-phosphate dehydrogenase (G6PD) measured in blood hemolysates (n=9/group). Data are expressed as mean ± SD normalized on hemoglobin (Hb) values (* < 0.05; ** < 0.01).

Journal: bioRxiv

Article Title: Integrated metabolic and proteostatic profiling reveals remodeling of proteolytic pathways associated with redox-bioenergetic dysfunction in a PAH enu2 mouse model of phenylketonuria

doi: 10.64898/2026.07.08.736353

Figure Lengend Snippet: HPLC quantification of (A) ATP, ADP, AMP, NAD, and NADH levels from WT and PKU mice; (B) reduced glutathione (GSH) and cysteine contents in whole blood (n=6/group). (C) Activities of glutathione peroxidase (GPX), glutathione reductase (GR), and glucose-6-phosphate dehydrogenase (G6PD) measured in blood hemolysates (n=9/group). Data are expressed as mean ± SD normalized on hemoglobin (Hb) values (* < 0.05; ** < 0.01).

Article Snippet: Detection was performed at 254 nm using a Jasco HPLC LC-net II (Jasco Inc., Japan).

Techniques: