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> Chemicals & Drugs > Amino Acid > Glycerol-3-Phosphate Dehydrogenase

Glycerol-3-Phosphate Dehydrogenase

Glycerol-3-Phosphate Dehydrogenase is an enzyme that plays a crucial role in lipid metabolism by catalyzing the reversible conversion of dihydroxyaceotne phosphate to glycerol-3-phosphate.
This reaction is an important step in the glycerol phosphate shuttle, which transports reducing equivalents between the cytoplasm and mitochondria.
Glycerol-3-Phosphate Dehydrogenase is found in a variety of organisms and tissues, and its dysregulation has been implicated in metabolic disorders such as diabetes and obesity.
Researchers can utilize PubCompare.ai's AI-powered optimization tools to discover reproducible, acurate research protocols for studying this key metabolic enzyme from the published literature, preprints, and patent records.

Most cited protocols related to «Glycerol-3-Phosphate Dehydrogenase»

1
Engineering Redox-Sensitive RoGFP Sensors
Cited 27 times
The RoGFP protein contains two engineered cysteine thiols, as first described by Remington et al. (RoGFP2) 11 (link). The cDNA encoding the protein was created by introducing four mutations in the mammalian GFP expression vector (pEGFP-N1) (C48S, Q80R, S147C, and Q204C) using a QuikChange Multi Site-directed mutagenesis kit (Strategene). The RoGFP construct was ligated into the VQ Ad5CMV K-NpA adenoviral shuttle vector between the KpnI and NotI sites; after sequencing and amplification this plasmid was used to generate a recombinant adenovirus to permit widespread expression in our cells (ViraQuest Inc., North Liberty, IA). The resulting redox-sensitive protein has excitation maxima at 400 and 484 nm, with emission at 525 nm. In response to changes in redox conditions, RoGFP exhibits reciprocal changes in intensity at the two excitation maxima 12 (link), and its ratiometric characteristics render it insensitive to expression levels 13 (link)-15 (link). Although RoGFP’s fluorescence behavior is relatively independent of pH and it does not respond to authentic nitric oxide (NO), reduced NADH, or the antioxidant N-acetyl-L-cysteine (NAC), its spectrum is slightly affected by reduced glutathione (GSH) possibly due to thiol-disulfide exchange (Online Figures I and II).
RoGFP was expressed in the mitochondrial matrix (Mito-RoGFP) by appending a 48 bp region encoding the mitochondrial targeting sequence from cytochrome oxidase subunit IV, at the 5′ end of the coding sequence. This construct was then ligated into the VQ Ad5CMV K-NpA plasmid between the KpnI and NotI sites, and used to generate an adenoviral vector. RoGFP was targeted to the mitochondrial inter-membrane space (IMS-RoGFP) by appending it to glycerol phosphate dehydrogenase (GPD). A cDNA construct encoding GPD, an integral protein of the inner mitochondrial membrane whose C-terminus protrudes into the inter-membrane space 17 (link), was ligated in-frame with cDNA encoding RoGFP 17 (link). The corresponding polypeptide includes amino acids 1–626 of GPD, with RoGFP at the carboxy terminus. This method has been used previously to express YFP in the inter-membrane space 18 (link). (See Online Supplemental Material for characterization of the RoGFP sensors and experimental protocols).
Waypa G.B., Marks J.D., Guzy R., Mungai P.T., Schriewer J., Dokic D, & Schumacker P.T. (2009). HYPOXIA TRIGGERS SUBCELLULAR COMPARTMENTAL REDOX SIGNALING IN VASCULAR SMOOTH MUSCLE CELLS. Circulation research, 106(3), 526-535.
Publication 2009
Acetylcysteine Adenoviruses Adenovirus Vaccine Amino Acids Antioxidants Cells Cloning Vectors Cysteine Cytochrome-c Oxidase Subunit IV Disulfides DNA, Complementary Fluorescence glycerol-1-phosphate dehydrogenase Glycerol-3-Phosphate Dehydrogenase Integral Membrane Proteins Mammals Mitochondria Mitochondrial Membrane, Inner Mitochondrial Membranes Mitomycin Mutagenesis, Site-Directed Mutation NADH Open Reading Frames Oxidation-Reduction Oxide, Nitric Plasmids Polypeptides Proteins Reading Frames Reduced Glutathione Shuttle Vectors Sulfhydryl Compounds Tissue, Membrane
2
Photosynthetic Enzyme Activity Assays
Cited 8 times
The activities of the photosynthetic enzymes Rubisco and PEPC were measured as previously described by Cousins et al. (2007) (link), with some changes. Frozen leaf tissue was processed in ice-cold glass homogenizers with 500 μl of extraction buffer (50 mM HEPES-KOH pH 7.8, 1 mM EDTA, 0.1% Triton-X, 10 mM dithiothreitol, and 1% polyvinylpolypyrrolidone) and 10 μl of protease inhibitor cocktail (Sigma). The homogenate was briefly centrifuged and the supernatant used for assays. For PEPC, 10 μl of leaf extract was combined with 980 μl of assay buffer (50 mM EPPS-NaOH pH 8, 10 mM MgCl2, 0.5 mM EDTA, 0.2 mM NADH, 5 mM glucose-6-phosphate 1 mM NaHCO3, and 1 U ml−1 malate dehydrogenase) and the reaction initiated by the addition of 10 μl of 400 mM PEP. For Rubisco, 10 μl of leaf extract was combined with 970 μl of assay buffer (50 mM EPPS-NaOH pH 8, 10 mM MgCl2, 0.5 mM EDTA, 1 mM ATP, 5 mM phosphocreatine, 20 mM NaHCO3, 0.2 mM NADH, 50 U ml−1 creatine phosphokinase, 0.2 mg carbonic anhydrase, 50 U ml−1 3-phosphoglycerate kinase, 40 U ml−1 glyceraldehyde-3-phosphate dehydrogenase, 113 U m;−1 Triose-phosphate isomerase, 39 U ml−1 glycerol 3 phosphate dehydrogenase) and the reaction initiated by the addition of 20 μl of 21.9 mM ribulose-1, 5-bisphosphate (RuBP). The activity of both enzymes was calculated by monitoring the decrease of NADH absorbance at 340 nm with a diode array spectrophotometer (Hewlett Packard) after initiation of the reaction.
Chlorophyll was extracted from frozen leaf discs in a glass homogenizer with 80% acetone. The chlorophyll a and b contents of extracts were measured in a quartz cuvette at 663.3 nm and 646.6 nm, and calculated according to Porra et al. (1989) .
Pengelly J.J., Sirault X.R., Tazoe Y., Evans J.R., Furbank R.T, & von Caemmerer S. (2010). Growth of the C4 dicot Flaveria bidentis: photosynthetic acclimation to low light through shifts in leaf anatomy and biochemistry. Journal of Experimental Botany, 61(14), 4109-4122.
Publication 2010
Acetone Bicarbonate, Sodium Biological Assay Buffers Chlorophyll Chlorophyll A Cold Temperature Creatine Kinase Dehydratase, Carbonate Dithiothreitol Edetic Acid enzyme activity Freezing Glucose-6-Phosphate Glyceraldehyde-3-Phosphate Dehydrogenases Glycerol-3-Phosphate Dehydrogenase HEPES Magnesium Chloride Malate Dehydrogenase NADH Phosphocreatine Phosphotransferases Photosynthesis Plant Leaves polyvinylpolypyrrolidone Protease Inhibitors Quartz ribulose Ribulose-Bisphosphate Carboxylase Tissues Triose-Phosphate Isomerase
3
Purification and Characterization of Chicken Muscle Triosephosphate Isomerase
Cited 7 times
Rabbit muscle glycerol 3-phosphate dehydrogenase (GPDH) was purchased from United States Biochemical or MP Biomedicals. Bovine serum albumin (BSA) was from Roche. DEAE Sepharose Fast Flow was from GE Healthcare. D,L-Glyceraldehyde 3-phosphate diethyl acetal (barium salt), dihydroxyacetone phosphate (lithium salt), Dowex 50WX4-200R and NADH (disodium salt) were from Sigma. Triethanolamine hydrochloride and imidazole were from Aldrich. Sodium phosphite (dibasic, pentahydrate) was from Riedel-de Haën (Fluka). [1-13C]-Glycolaldehyde (99% enriched with 13C at C-1, 0.09 M in water) was purchased from Omicron Biochemicals. D2O (99.9% D) and DCl (35% w/w, 99.9% D) were from Cambridge Isotope Laboratories. Imidazole was recrystallized from benzene. Water was from a Milli-Q Academic purification system. All other commercially available chemicals were reagent grade or better and were used without further purification.
The plasmid pBSX1cTIM containing the wild-type gene for TIM from chicken muscle (25 (link)) and E. coli strain DF502 (strepR, tpi-, and his-) whose DNA lacks the gene for TIM (26 (link)) were generous gifts from Professor Nicole Sampson. E. coli strain DF502 was transformed with pBSX1cTIM and TIM was expressed and purified according to published procedures with ion exchange chromatography performed on DEAE sepharose (15 (link)). The enzyme obtained from the final column was judged to be homogeneous by gel electrophoresis. The concentration of TIM was determined from the absorbance at 280 nm using an extinction coefficient of 3.2 × 104 M-1 cm-1 (27 (link)). The following kinetic parameters were determined for turnover of GAP in 30 mM triethanolamine buffer at pH 7.5 and 25 °C (I = 0.1, NaCl) using a coupled assay (see below): kcat = 2300 s-1 and Km = 0.45 mM (22 (link)).
Go M.K., Amyes T.L, & Richard J.P. (2009). Hydron Transfer Catalyzed by Triosephosphate Isomerase. Products of the Direct and Phosphite-Activated Isomerization of [1-13C]-Glycolaldehyde in D2O. Biochemistry, 48(24), 5769-5778.
Publication 2009
2-diethylaminoethanol Acetals Barium Benzene Biological Assay Buffers Chickens CM 2-3 Dihydroxyacetone Phosphate Dowex Electrophoresis Enzymes Escherichia coli Extinction, Psychological Genes Gifts Glyceraldehyde 3-Phosphate Glycerol-3-Phosphate Dehydrogenase glycolaldehyde imidazole Ion-Exchange Chromatographies Isotopes Kinetics Lithium Muscle Tissue NADH Phosphite Plasmids Rabbits Sepharose Serum Albumin, Bovine Sodium Sodium Chloride Strains triethanolamine triethanolamine hydrochloride
4
Characterization of H9N2 Avian Influenza Virus
Cited 5 times
H9N2 AIV used in this study was isolated from the cloaca of the healthy chicken in Shandong 2017, which was collected as samples of routinely ongoing surveillance. The hemagglutination inhibition with the special antibody confirmed that the isolate might be H9N2 subtype AIV. The virus was thrice propagated in 9-day-old specific-pathogen-free (SPF) embryonated chicken eggs, and then gene fragments were sequenced and comparatively analyzed. Madin-Darbycanine kidney (MDCK) cells were maintained in Dulbecco modified Eagle medium (DMEM) supplemented with 10% fetal bovine serum (FBS) and 5% CO2 at 37 °C.
Anti-vimentin monoclonal antibody was purchased from Abcam (ab45939) and anti-hemagglutinin polyclonal antibody was purchased from Jianchun Biotechnology (Nanjing). Anti- Glycerophosphate dehydrogenase (GAPDH) antibody (ab8245) was purchased from Abcam. Alkaline phosphatase conjugated goat anti-rabbit IgG and HRP-conjugated goat anti-mouse IgG secondary antibody was purchased from Univ Biotechnology (Shanghai). Vimentin siRNA was purchased from Santa Cruz (sc-156,015).
Yu Y.N., Zheng Y., Hao S.S., Zhang Z., Cai J.X., Zong M.M., Feng X.L, & Liu Q.T. (2020). The molecular evolutionary characteristics of new isolated H9N2 AIV from East China and the function of vimentin on virus replication in MDCK cells. Virology Journal, 17, 78.
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Publication 2020
Alkaline Phosphatase anti-IgG Antibodies, Anti-Idiotypic Cells Chickens Eagle Eggs Enterobacter Fetal Bovine Serum GAPDH protein, human Genes Glycerol-3-Phosphate Dehydrogenase Goat Hemagglutination Inhibition Tests Hemagglutinin Immunoglobulins Kidney Monoclonal Antibodies Mus Rabbits RNA, Small Interfering Specific Pathogen Free Vimentin Virus
5
Transcriptional Analysis of Cellulase and Trehalose Biosynthesis in Trichoderma reesei
Cited 5 times
Total RNA was extracted from T. reesei Δku70 or Δtmk3 strain growing in solid state media and submerged media containing 2% avicel and 2% wheat bran for the examination of expression of cellulase-, hemicellulase-, chitin synthase- and β-1,3-glucan synthase-coding genes, as well as from T. reesei Δku70 or Δtmk3 strain growing in submerged media containing 2% glucose and 0 or 0.15 M NaCl for the examination of expression of glycerol-3-phosphate dehydrogenase- and α,α -trehalose-6-phosphate synthase-coding genes. cDNA was synthesized using PrimeScript RT reagent kit with gDNA erase (Perfect Real Time) from Takara Bio Inc. (Shiga, Japan).
Real-time PCR reactions were carried out on a LightCycler 480II Real-Time PCR system (Roche Applied Science, Mannheim, Germany) using SYBR Premix EX TaqTM II (Takara Bio Inc., Shiga, Japan) as the dye. Three individual biological replicates and three individual technical replicates for each biological sample (a total of 9 replicates for each reaction) were carried out. The relative abundance of genes was calculated using the 2−ΔΔCt method as previously described [45] (link).
Wang M., Zhao Q., Yang J., Jiang B., Wang F., Liu K, & Fang X. (2013). A Mitogen-Activated Protein Kinase Tmk3 Participates in High Osmolarity Resistance, Cell Wall Integrity Maintenance and Cellulase Production Regulation in Trichoderma reesei. PLoS ONE, 8(8), e72189.
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Publication 2013
Avicel Biopharmaceuticals Cellulase Chitin Synthase DNA, Complementary Genes glucan synthase Glucose Glycerol-3-Phosphate Dehydrogenase hemicellulase Sodium Chloride Strains trehalose-6-phosphate synthase Wheat Bran

Most recents protocols related to «Glycerol-3-Phosphate Dehydrogenase»

1
Enzymatic Assay for Fructose-1,6-Bisphosphate
The assay was carried out according to the method described earlier (50 (link)). The reaction mixture contained 50 mM Tris–HCl, 0.1 M potassium acetate buffer (pH 8.0), 0.1–5 mM FBP, 0.2 mM NADH, and a mixture of coupling enzymes, glycerol phosphate dehydrogenase, and triosephosphate isomerase. The reaction was initiated by the addition of retina lysate and we monitored the decrease in the absorbance at 340 nm from the oxidation of NADH.
Rajala A., Bhat M.A., Teel K., Gopinadhan Nair G.K., Purcell L, & Rajala R.V. (2023). The function of lactate dehydrogenase A in retinal neurons: implications to retinal degenerative diseases. PNAS Nexus, 2(3), pgad038.
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Publication 2023
Biological Assay Buffers Enzymes Glycerol-3-Phosphate Dehydrogenase NADH Potassium Acetate Retina Triose-Phosphate Isomerase Tromethamine
2
Antioxidant Capacity Evaluation of Crayfish
The hepatopancreas and ovary tissues were weighed and homogenized in precooled saline solution with 10-fold volumes (v/w). These homogenates were centrifuged at 3,500 rpm in 4°C for 10 min (3-18KS, Sigma, Germany) and the supernatants were collected. The supernatants of the hepatopancreas and ovaries and serum were diluted with 0.85% saline solution and follow the instruction and preexperiment for subsequent operations.
The supernatants of hepatopancreas and ovary homogenates were taken to determine the contents of triacylglycerol (TG) (glycerophosphate oxidase-peroxidase method) [23 (link), 24 (link)] and total cholesterol (T-CHO) (cholesterol oxidase-peroxidase method) [25 (link)]. The concentrations of high-density lipoprotein cholesterol (HDL-C), low-density lipoprotein cholesterol (LDL-C) (enzymatic method) [26 (link), 27 (link)], malondialdehyde (MDA) (thiobarbituric acid method) [28 (link)], glutathione peroxidase (GSH-Px) (5, 5′-dithiobis-(2-nitrobenzoic acid) method) [29 (link)], superoxide dismutase (SOD) (hydroxylamine method) [30 (link)], and total antioxidant capacity (T-AOC) (Fe3+ reduction method) [31 (link)] were detected to evaluate the antioxidant capacity of crayfish fed diets with different phospholipids. All detection was performed by the colorimetric approach of commercial reagent kits (Nanjing Jiancheng Bioengineering Institute, China). The measurements of these parameters were performed by the standard method, and the detection of optical density (OD) values was analyzed by a microplate reader (Epoch, BioTek, USA).
Xu C., Yang X., Liang Z., Jiang Z., Chen H., Han F., Jia Y, & Li E. (2023). Evaluation of the Role of Soybean Lecithin, Egg Yolk Lecithin, and Krill Oil in Promoting Ovarian Development in the Female Redclaw Crayfish Cherax quadricarinatus. Aquaculture Nutrition, 2023, 6925320.
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Publication 2023
Antioxidants Astacoidea Cholesterol Cholesterol, beta-Lipoprotein Cholesterol Oxidase Colorimetry Diet Enzymes EPOCH protocol Glycerol-3-Phosphate Dehydrogenase Hepatopancreas High Density Lipoprotein Cholesterol Hydroxylamine Malondialdehyde Nitrobenzoic Acids Ovary Peroxidase Peroxidase, Glutathione Phospholipids Saline Solution Serum Superoxide Dismutase thiobarbituric acid Tissues Triglycerides Vision
3
Cardiometabolic Risk Factors Evaluation
Hypertension was defined as currently using antihypertensive medicine and/or an average of three sitting systolic blood pressure (SBP) measurements ≥140 mmHg and/or an average of three sitting diastolic blood pressure measurements ≥90 mmHg after at least a 5‐min rest and with a 30‐s interval. Total cholesterol (TC), triglyceride (TG), and high‐density lipoprotein cholesterol (HDL‐C) were assessed on a Hitachi 7060 Clinical Analyzer (Hitachi High‐Technologies Corp., Tokyo, Japan) with cholesterol oxidase method, glycerophosphate oxidase method, and direct chemically modified enzyme method, respectively.22 Low‐density lipoprotein cholesterol (LDL‐C) levels were calculated using the Friedewald formula (LDL‐C = TC − HDL‐C − TG/5) for the participants whose TG levels were <400 mg/dl.23 Dyslipidemia was defined as currently using lipid‐lowering drugs, and/or TC ≥240 mg/dl, and/or TG ≥200 mg/dl, and/or LDL‐C ≥160 mg/dl, and/or HDL‐C <40 mg/dl after fasting for at least 10 h.24 Body mass index (BMI) was calculated as weight (kg)/height (m)2.
Other known or suspected risk factors for CVD, including demographic characteristics, lifestyle, medical history of chronic diseases, and family history of CVD, were collected using structured questionnaires face to face at each visit by trained data investigators. Age (in years), smoking status (never smoker, former smoker, current smoker), drinking status (current drinker or not), educational level (no education history, primary school, middle school, high school, college or above), monthly household income per capita (<300, 300–500, 500–800, 800–1200, 1200–2000, ≥2000 Chinese yuan [CNY]/month), and physical activity level (whether or not the ideal level was reached during the previous 12 months) were assessed with standardized questionnaires. The definition of ideal physical activity level was at least 150 min of moderate‐intensity physical activity or at least 75 min of vigorous‐intensity physical activity per week, which was recommended by World Health Organization.25 Ideal vegetable and fruit intake was defined as at least 500 g per day according to the dietary guidelines for Chinese residents.26
Tong Y., Liu F., Huang K., Li J., Yang X., Chen J., Liu X., Cao J., Chen S., Yu L., Zhao Y., Wu X., Zhao L., Li Y., Hu D., Huang J., Lu X., Shen C, & Gu D. (2023). Changes in fasting blood glucose status and incidence of cardiovascular disease: The China‐PAR project. Journal of Diabetes, 15(2), 110-120.
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Publication 2023
Antihypertensive Agents Chinese Cholesterol Cholesterol, beta-Lipoprotein Cholesterol Oxidase Disease, Chronic Dyslipidemias Enzymes Face Fruit Glycerol-3-Phosphate Dehydrogenase Head High Blood Pressures High Density Lipoprotein Cholesterol Households Hypolipidemic Agents Index, Body Mass Pressure, Diastolic Systolic Pressure Triglycerides Vegetables
4
RuBisCO Activity Quantification in Lima Beans
Enzyme extraction and purification were conducted at 4 °C. A ratio of 1:6 (w/v) cold extraction buffer (50 mM NaOH-Bicine pH 8.2, 20 mM MgCl2, 1 mM EDTA, 2 mM Benzamidine, 5 mM aminocaproic acid, 50 mM 2-mercaptoethanol, 10 mM DL-dithiothreitol (DTT), 1 mM phenylmethylsulfonyl fluoride (PMSF)) was added to samples of 40 mg (1:12.5 w/v) of GMF- or NNMF-exposed Lima beans that were previously grinded in liquid nitrogen. The homogenate was then centrifuged at 14,000× g for 5 min at 4 °C. The supernatant was transferred to a new ice-cold tube and immediately used for the RuBisCO activity assay.
The assay was carried out in a Microplate reader (NB-12-0035 Neo Biotech, Nanterre, FR). In flat bottom 96-well polystyrene microplates, 159.9 µL of mQ water for the blank and 153.9 µL for the samples were pipetted into each well, followed by a 35.1 µL assay mix (100 mM NaOH-Bicine pH 8.2, 20 mM MgCl2, 10 mM NaHCO3, 20 mM KCl, 5 mM DTT, 2 UI 3-Phosphoglyceric phosphokinase, 0.4 UI α-Glycerophosphate Dehydrogenase, 24 UI Triosephosphate isomerase, 2.8 UI Glyceraldehyde 3-Phosphate Dehydrogenase, 3 mM ATP, 1 mM NADH) avoiding exposure to light. Next, 5 µL of a sample supernatant were added to the wells. Then, 6 µL 20 mM RuBP (ribulose-1,5-bisphosphate) were added to start RubisCO activity. Then, 5 µL of the sample supernatant were added to the wells. The Microplate reader was set at 30 °C and absorbance was read at 340 nm. The calculation of RubisCO activity was carried out according to Sales and co-workers [80 ].
Parmagnani A.S., Betterle N., Mannino G., D’Alessandro S., Nocito F.F., Ljumovic K., Vigani G., Ballottari M, & Maffei M.E. (2023). The Geomagnetic Field (GMF) Is Required for Lima Bean Photosynthesis and Reactive Oxygen Species Production. International Journal of Molecular Sciences, 24(3), 2896.
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Publication 2023
2-Mercaptoethanol 6-Aminocaproic Acid benzamidine Bicarbonate, Sodium Biological Assay Buffers Cold Temperature Dithiothreitol Edetic Acid Enzymes Glyceraldehyde-3-Phosphate Dehydrogenases Glycerol-3-Phosphate Dehydrogenase Light Magnesium Chloride N,N-bis(2-hydroxyethyl)glycine NADH Nitrogen Phenylmethylsulfonyl Fluoride Phosphoglycerate Kinase Polystyrenes ribulose Ribulose-Bisphosphate Carboxylase Triose-Phosphate Isomerase Workers
5
Extraction and Assay of RubisCO Activity
Enzyme extraction and purification were conducted at 4 °C. A ratio of 1:6 (w/v) cold extraction buffer (50 mM NaOH-Bicine pH 8.2, 20 mM MgCl2, 1 mM EDTA, 2 mM Benzamidine, 5 mM aminocaproic acid, 50 mM 2-mercaptoethanol, 10 mM DL-dithiothreitol (DTT), 1 mM phenylmethylsulfonyl fluoride (PMSF)) was used to extract healthy, TSSM-infested Lima bean leaves and TSSMs that were ground in liquid nitrogen was added. The homogenate was then centrifuged at 14,000 g for 1 min at 4 °C. The supernatant was transferred to a new ice-cold tube and immediately used for the RubisCO activity assay.
The assay was carried out in a Microplate reader (NB-12-0035 Neo Biotech, Nanterre, France). In flat bottom 96-well polystyrene microplates, 159.9 µL of mQ water for the blank and 153.9 µL for the samples were pipetted into each well, followed by 35.1 µL assay mix (100 mM NaOH-Bicine pH 8.2, 20 mM MgCl2, 10 mM NaHCO3, 20 mM KCl, 5 mM DTT, 2 UI 3-Phosphoglyceric phosphokinase, 0.4 UI α-Glycerophosphate Dehydrogenase, 24 UI Triosephosphate isomerase, 2.8 UI Glyceraldehyde 3-Phosphate Dehydrogenase, 3 mM ATP, 1 mM NADH) avoiding exposure to light. Six µL 20 mM RuBP was added to start RubisCO activity. Then, 5 µL of sample supernatant was added to the wells. The Microplate reader was set at 30 °C, and absorbance was read at 340 nm. The calculation of RubisCO activity was carried out according to Sales et al. [56 ].
Parmagnani A.S., Mannino G., Brillada C., Novero M., Dall’Osto L, & Maffei M.E. (2023). Biology of Two-Spotted Spider Mite (Tetranychus urticae): Ultrastructure, Photosynthesis, Guanine Transcriptomics, Carotenoids and Chlorophylls Metabolism, and Decoyinine as a Potential Acaricide. International Journal of Molecular Sciences, 24(2), 1715.
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Publication 2023
2-Mercaptoethanol 6-Aminocaproic Acid benzamidine Bicarbonate, Sodium Biological Assay Buffers Cold Temperature Dithiothreitol Edetic Acid Enzymes Glyceraldehyde-3-Phosphate Dehydrogenases Glycerol-3-Phosphate Dehydrogenase Light Magnesium Chloride N,N-bis(2-hydroxyethyl)glycine NADH Nitrogen Phenylmethylsulfonyl Fluoride Phosphoglycerate Kinase Polystyrenes Ribulose-Bisphosphate Carboxylase Triose-Phosphate Isomerase

Top products related to «Glycerol-3-Phosphate Dehydrogenase»

1
Aldolase by Merck Group
Sourced in United States, Germany
Aldolase is a laboratory enzyme that catalyzes the reversible aldol reaction, which is a fundamental step in carbohydrate metabolism. It plays a crucial role in the glycolytic pathway by facilitating the conversion of fructose-1,6-bisphosphate to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate.
2
Glycerol 3 phosphate dehydrogenase by Merck Group
Sourced in Japan, United States
Glycerol-3-phosphate dehydrogenase is an enzyme that catalyzes the reversible oxidation of glycerol-3-phosphate to dihydroxyacetone phosphate. It is involved in glycolysis and gluconeogenesis pathways.
3
Triosephosphate isomerase by Merck Group
Sourced in United States
Triosephosphate isomerase is a laboratory enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate, which are important intermediates in the glycolysis pathway. This enzyme plays a crucial role in the breakdown of glucose to generate energy for cellular processes.
4
Adenosine triphosphate (atp) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Sao Tome and Principe, Italy, Japan, Macao, Spain, Canada, France, Switzerland, Ireland, Sweden, Australia
ATP is a laboratory instrument used to measure the presence and concentration of adenosine triphosphate (ATP) in various samples. ATP is a key molecule involved in energy transfer within living cells. The ATP product provides a reliable and accurate method for quantifying ATP levels, which is useful in applications such as microbial detection, cell viability assessment, and ATP-based assays.
5
Trizol reagent by Thermo Fisher Scientific
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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.
6
Reduced nicotinamide adenine dinucleotide nadh by Roche
Sourced in Germany
Reduced nicotinamide adenine dinucleotide (NADH) is a coenzyme found in living cells. It is the reduced form of nicotinamide adenine dinucleotide (NAD+) and plays a crucial role in cellular metabolism, serving as an electron carrier in various enzymatic reactions.
7
Immobilized metal affinity chromatography resin by Bio-Rad
Sourced in United States
Immobilized Metal Affinity Chromatography (IMAC) resin is a chromatographic material used for the purification of proteins and other biomolecules. It consists of a solid support matrix with immobilized metal ions, typically nickel or cobalt, which can selectively bind to specific amino acid residues present in the target biomolecules. The core function of IMAC resin is to facilitate the separation and purification of these biomolecules from complex mixtures.
8
Amicon ultra 30 kda filters by Merck Group
Sourced in United States
The Amicon Ultra 30 kDa filters are a type of centrifugal filter device used for the concentration and purification of macromolecules, such as proteins, from solutions. The filters have a molecular weight cutoff of 30 kDa, which means they can retain molecules larger than 30 kDa while allowing smaller molecules to pass through. The filters are designed for efficient sample recovery and can be used in a variety of laboratory applications.
9
Au5400 system by Olympus
Sourced in Japan
The AU5400 system is a fully automated clinical chemistry analyzer designed for high-volume testing in medical laboratories. It features a compact, modular design and offers a range of analytical capabilities for the quantitative determination of various analytes in biological samples.
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High capacity cdna reverse transcription kit by Thermo Fisher Scientific
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The High-Capacity cDNA Reverse Transcription Kit is a laboratory tool used to convert RNA into complementary DNA (cDNA) molecules. It provides a reliable and efficient method for performing reverse transcription, a fundamental step in various molecular biology applications.

More about "Glycerol-3-Phosphate Dehydrogenase"

Glycerol-3-phosphate dehydrogenase (G3PDH or GPDH) is a crucial enzyme in lipid metabolism, catalyzing the reversible conversion of dihydroxyacetone phosphate to glycerol-3-phosphate.
This reaction is a key step in the glycerol phosphate shuttle, which transports reducing equivalents between the cytoplasm and mitochondria.
G3PDH is found in a variety of organisms and tissues, and its dysregulation has been implicated in metabolic disorders like diabetes and obesity.
Researchers can leverage PubCompare.ai's AI-powered optimization tools to uncover reproducible, accurate research protocols for studying this important metabolic enzyme.
By comparing published literature, preprints, and patent records, the platform can help identify the optimal solutions for your research needs.
In addition to G3PDH, related enzymes and molecules like aldolase, triosephosphate isomerase, ATP, NADH, and TRIzol reagent may also be relevant to your investigations.
Techniques such as immobilized metal affinity chromatography (IMAC) and Amicon Ultra 30 kDa filters can be used for protein purification and concentration, while the AU5400 system and High-Capacity cDNA Reverse Transcription Kit can aid in downstream analysis.
By combining the power of AI-driven optimization with a comprehensive understanding of the key players in glycerol-3-phosphate metabolism, you can unlock new insights and advance your research on this crucial enzyme.