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Pyridoxal Phosphate

Pyridoxal Phosphate is a coenzyme form of vitamin B6 that plays a crucial role in numerous metabolic processes within the body.
It serves as a cofactor for various enzymes involved in the metabolism of amino acids, lipids, and carbohydrates.
Pyridoxal Phosphate is essential for the proper functioning of the nervous system, the immune system, and the development of red blood cells.
Researching the role of Pyridoxal Phosphate in health and disease can provide valuable insights into a wide range of physiological and pathological conditions.
Optimizing research protocols for reproducibilty and accuracy is crucial when investigating this important biomolecule.

Most cited protocols related to «Pyridoxal Phosphate»

Comprehensive Biomarker Assessment Protocol

Detailed methodology is included in Additional File 1. Blood samples were analyzed for complete blood counts, creatinine, albumin, plasma lipids, total carotenoids, vitamin C, folate, vitamin B12, pyridoxal-5'-phosphate, homocysteine, methylmalonic acid, C-reactive protein, glucose, insulin, glycosylated hemoglobin, blood urea nitrogen, and dehydroepiandrosterone sulfate. A 12-hour urine sample was analyzed for cortisol, creatinine, epinephrine and norepinephrine. Saliva samples were used for measurement of salivary cortisol.

Tucker K.L., Mattei J., Noel S.E., Collado B.M., Mendez J., Nelson J., Griffith J., Ordovas J.M, & Falcon L.M. (2010). The Boston Puerto Rican Health Study, a longitudinal cohort study on health disparities in Puerto Rican adults: challenges and opportunities. BMC Public Health, 10, 107.

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Publication 2010

Albumins Ascorbic Acid BLOOD Carotenoids Cobalamins Complete Blood Count C Reactive Protein Creatinine Dehydroepiandrosterone Sulfate Epinephrine Folate Glucose Hemoglobin, Glycosylated Homocysteine Hydrocortisone Insulin Lipids Methylmalonic Acid Norepinephrine Plasma Pyridoxal Phosphate Saliva Urea Nitrogen, Blood Urine

Overexpressing Soybean Salt Tolerance Gene GmCHX1

The full-length coding sequence of GmCHX1 from W05 was cloned into the binary vector V7 (ref. 56 (link)) between XbaI and XhoI sites downstream of the constitutive Cauliflower Mosaic Virus 35S promoter. As a negative control, the gene for the GFP was cloned instead of GmCHX1 using the same vector and promoter. Both constructs were then transformed into the salt-sensitive parent C08. The soybean hairy root transformation and salt treatments were performed as previously described57 with some modifications. Surface-sterilized soybean seeds were germinated on germination medium (15 mg l⁻¹ NaH₂PO₄·H₂O, 1 mM CaCl₂·2H₂O, 25 mM KNO₃, 1 mM (NH₄)₂SO₄, 1 mM MgSO₄·7H₂O, 0.1 mM Na₂EDTA·2H₂O, 0.1 mM FeSO₄·7H₂O, 10 mg l⁻¹ MnSO₄·2H₂O, 2 mg l⁻¹ ZnSO₄·7H₂O, 3 mg l⁻¹ H₃BO₃, 0.25 mg l⁻¹ Na₂MoSO₄·2H₂O, 0.025 mg l⁻¹ CuSO₄·5H₂O, 0.025 mg l⁻¹ CoCl₂·6H₂O, 0.75 mg l⁻¹ KI, 1 × B5 vitamin (10 mg l⁻¹ thiamine, 1 mg l⁻¹ pyridoxal phosphate, 1 mg l⁻¹ nicotinic acid and 100 mg l⁻¹ myo-inositol), 2% sucrose, 0.6% agar, pH 5.8) for 4 days (16 h light/8 h dark). Agrobacterium rhizogenes strain K599 containing the recombinant constructs was grown in yeast extract peptone medium containing 50 mg l⁻¹ kanamycin and 200 μM acetosyringone at 28 °C for 16 h. It was then used to infect the cotyledons through scalpel incisions. The cotyledons were co-cultivated with A. rhizogenes in the dark for 5 days on moist filter paper. After that, the infected cotyledons were transferred to root-inducing medium (4.3 g l⁻¹ Murashige and Skoog (MS) medium, 1 × B5 vitamin, 3% sucrose, 250 mg l⁻¹ cefotaxime and 50 mg l⁻¹ kanamycin). After 2 weeks, cotyledons with roots emerging from the incision sites were transferred to new root-inducing medium with 100 mM NaCl or medium without NaCl as untreated control. Root mass was weighed about 2 weeks after treatment.

Qi X., Li M.W., Xie M., Liu X., Ni M., Shao G., Song C., Kay-Yuen Yim A., Tao Y., Wong F.L., Isobe S., Wong C.F., Wong K.S., Xu C., Li C., Wang Y., Guan R., Sun F., Fan G., Xiao Z., Zhou F., Phang T.H., Liu X., Tong S.W., Chan T.F., Yiu S.M., Tabata S., Wang J., Xu X, & Lam H.M. (2014). Identification of a novel salt tolerance gene in wild soybean by whole-genome sequencing. Nature Communications, 5, 4340.

Publication 2014

acetosyringone Agar Agrobacterium rhizogenes Cauliflower Mosaic Virus Cefotaxime Cloning Vectors Cotyledon Genes Germination Hair Inositol Kanamycin Light Niacin Open Reading Frames Pantothenic Acid Parent Peptones Plant Embryos Plant Roots Pyridoxal Phosphate Sodium Chloride Soybeans Strains Sucrose Sulfate, Magnesium Thiamine Yeast, Dried

Enzymatic Assays for Cholinergic and Dopaminergic Activities

Cells were harvested as described above and were disrupted by homogenization in a ground-glass homogenizer fitted with a ground-glass pestle, using a buffer consisting of 154 mM NaCl and 10 mM sodium-potassium phosphate (pH 7.4). Aliquots were withdrawn for measurement of DNA and protein (Smith et al. 1985 (link)).
ChAT assays (Lau et al. 1988 (link)) were conducted in 60 μL of a buffer consisting of 60 mM sodium phosphate (pH 7.9), 200 mM NaCl, 20 mM choline chloride, 17 mM MgCl₂, 1 mM EDTA, 0.2% Triton X-100, 0.12 mM physostigmine, and 0.6 mg/mL bovine serum albumin (Sigma Chemical Co.), containing a final concentration of 50 μM [¹⁴C]acetyl-coenzyme A (specific activity 60 mCi/mmol, diluted with unlabeled compound to 6.7 mCi/mmol; PerkinElmer Life Sciences, Boston, MA). The amount of protein used in each assay was adjusted to maintain activity within the linear range. Blanks contained homogenization buffer instead of the tissue homogenate. Samples were pre-incubated for 15 min on ice and transferred to a 37°C water bath for 30 min; the reaction was terminated by placing the samples on ice. Labeled acetylcholine was then extracted and counted in a liquid scintillation counter and the activity was calculated as nanomoles synthesized per hour per microgram DNA.
TH activity was measured using [¹⁴C]tyrosine as a substrate and trapping the evolved ¹⁴CO₂ after coupled decarboxylation with dopa decarboxylase (Lau et al. 1988 (link); Waymire et al. 1971 (link)). Homogenates were sedimented at 26,000 × g for 10 min to remove storage vesicles containing catecholamines, which interfere with TH activity, and assays were conducted with 100 μL aliquots of the supernatant solution in a total volume of 550 μL. Each assay (pH 6.1) contained final concentrations of 910 μM FeSO₄, 55 μM unlabeled L-tyrosine (Sigma Chemical Co.), 9.1 μM pyridoxal phosphate (Sigma Chemical Co.), 36 μM β-mercaptoethanol, and 180 μM 2-amino-6,7-dimethyl-4-hydroxy-5,6,7,8-tetrahydropteridine HCl (Sigma Chemical Co.), all in a buffer of 180 mM sodium acetate and 1.8 mM sodium phosphate (pH 6.1). Each assay contained 0.5 μCi of generally labeled [¹⁴C]tyrosine (specific activity, 438 mCi/mmol; Sigma Chemical Co.) as substrate, and blanks contained buffer in place of the homogenate. Activity was calculated on the same basis as for ChAT.

Slotkin T.A., MacKillop E.A., Ryde I.T., Tate C.A, & Seidler F.J. (2006). Screening for Developmental Neurotoxicity Using PC12 Cells: Comparisons of Organophosphates with a Carbamate, an Organochlorine, and Divalent Nickel. Environmental Health Perspectives, 115(1), 93-101.

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Publication 2006

2-Mercaptoethanol 5,6,7,8-tetrahydropteridine Acetylcholine Bath Biological Assay Buffers Catecholamines Cells Choline Chloride Coenzyme A, Acetyl Decarboxylation Dopa Decarboxylase Edetic Acid Magnesium Chloride Physostigmine Potassium potassium phosphate Proteins Pyridoxal Phosphate Scintillation Counters Serum Albumin, Bovine Sodium Sodium Acetate Sodium Chloride sodium phosphate Tissues Triton X-100 Tyrosine

Enzymatic Assays for Cholinergic and Dopaminergic Activity

Cells were harvested as described above and were disrupted by homogenization in a ground-glass homogenizer fitted with a ground-glass pestle, using a buffer consisting of 154 mM NaCl and 10 mM sodium-potassium phosphate (pH 7.4). An aliquot was withdrawn for measurement of protein (Smith et al. 1985 (link)).
ChAT assays (Lau et al. 1988 (link)) were conducted with 40 μg of sample protein in 60 μL of a buffer consisting of 60 mM sodium phosphate (pH 7.9), 200 mM NaCl, 20 mM choline chloride, 17 mM MgCl₂, 1 mM EDTA, 0.2% Triton X-100, 0.12 mM physostigmine (Sigma), and 0.6 mg/mL bovine serum albumin (Sigma), containing a final concentration of 50 μM [¹⁴C]acetyl-coenzyme A (specific activity of 44 mCi/mmol, diluted with unlabeled compound to 6.7 mCi/mmol; PerkinElmer Life Sciences, Boston, MA). Blanks contained homogenization buffer instead of the tissue homogenate. Samples were preincubated for 15 min on ice, transferred to a 37°C water bath for 30 min, and the reaction terminated by placing the samples on ice. Labeled acetylcholine was then extracted and counted in a liquid scintillation counter, and the activity was determined relative to DNA or protein.
TH activity was measured using [¹⁴C]tyrosine as a substrate and trapping the evolved ¹⁴CO₂ after coupled decarboxylation with DOPA decarboxylase (Lau et al. 1988 (link); Waymire et al. 1971 (link)). Homogenates were sedimented at 26,000 × g for 10 min to remove storage vesicles containing catecholamines, which interfere with TH activity, and assays were conducted with 100 μL aliquots of the supernatant solution in a total volume of 550 μL. Each assay contained final concentrations of 910 μM FeSO₄, 55 μM unlabeled l-tyrosine (Sigma), 9.1 μM pyridoxal phosphate (Sigma), 36 μM β-mercaptoethanol, and 180 μM 2-amino-6,7-dimethyl-4-hydroxy-5,6,7,8-tetrahydropteridine HCl (Sigma), all in a buffer of 180 mM sodium acetate and 1.8 mM sodium phosphate (pH 6.1). Each assay contained 0.5 μCi of generally labeled [¹⁴C]tyrosine (specific activity, 438 mCi/mmol; Sigma) as substrate, and blanks contained buffer in place of the homogenate.

Jameson R.R., Seidler F.J., Qiao D, & Slotkin T.A. (2005). Chlorpyrifos Affects Phenotypic Outcomes in a Model of Mammalian Neurodevelopment: Critical Stages Targeting Differentiation in PC12 Cells. Environmental Health Perspectives, 114(5), 667-672.

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Publication 2005

Standardized Hepatitis C Biomarker Analysis

The serum of 24 informed patients (21 with chronic hepatitis C and 3 with decompensated alcoholic cirrhosis) were prospectively collected in the Department of Hepato-Gastroenterology of the Pitié-Salpêtrière Hospital, in Paris, France. The main characteristics of the included patients are outlined in Table 1. Sera were separated in the above reference laboratory, conserved at + 4°C and distributed to ten different laboratories, in France, within 24 hours. For two laboratories, serum was missing for at least one patient; therefore, these laboratories have been excluded from the core analysis. Sensitivity analyses including these two excluded laboratories did not change the results or conclusions (data not shown).
Characteristics of the analyzer, reagents and analytical methods employed used in the nine included laboratories are detailed in Table 4. Eleven different analyzers were used. For the measurement of ALT activity, five laboratories used a standardized method according to the IFCC, with pyridoxal phosphate, and four without pyridoxal phosphate. For the measurement of GGT activity, the nine laboratories used the Szasz method; including in four a recommended method of standardization [11 (link)].
Haptoglobin and apolipoprotein A1 were assayed by immunoturbidimetric or immunonephelemetric methods. α₂-macroglobulin was assayed by immunonephelemetry. Analytical measurements of α₂-macroglobulin and haptoglobin were standardized against the certified international reference material 470 (CRM 470). Apolipoprotein A1 assays adapted on the different analyzers were standardized against the reference material of World Health Organization-International Federation of Clinical Chemistry SP1-01 (WHO-IFCC SP1-01), except on the Advia-Bayer-analyzer (ADVIA). Total bilirubin was assayed by diazoreactions methods.
Statistical analysis used multiple measure variance analyses and Passing-Bablok linear regression analyses for the comparison of inter-laboratory results, and kappa statistics for the predicted histological features. Multiple comparisons used Bonferroni (versus control) and Tukey-Kramer multiple-comparison tests. Number Cruncher Statistical Systems software was used [12 ]. The linear relationship between laboratories and reference center were assessed with confidence limits for the slope and the intercept and the number of pairs out of bounds; they were used to determine whether there was only a chance difference between the slope and 1 and between the intercept and 0 [13 (link)]. Means were expressed with standard deviation (sd), except for kappa statistics.

Halfon P., Imbert-Bismut F., Messous D., Antoniotti G., Benchetrit D., Cart-Lamy P., Delaporte G., Doutheau D., Klump T., Sala M., Thibaud D., Trepo E., Thabut D., Myers R.P, & Poynard T. (2002). A prospective assessment of the inter-laboratory variability of biochemical markers of fibrosis (FibroTest) and activity (ActiTest) in patients with chronic liver disease. Comparative Hepatology, 1, 3.

Publication 2002

alpha 2-Glucoproteins Apolipoprotein A-I Bilirubin Haptoglobins Hepatitis C, Chronic Hypersensitivity Liver Cirrhosis, Alcoholic Patients Pyridoxal Phosphate Serum

Most recents protocols related to «Pyridoxal Phosphate»

Liver Injury Biomarker Ratio Calculation

Serum ALT and LDH levels were measured using the 7500 Clinical Analyzer (Hitachi High-Technologies Corporation, Tokyo, Japan). LDH was assayed using an enzymatic rate method with lactate as a substrate, and we confirmed that the origin of LDH was mainly from liver tissue using the LDH isozymes test. ALT assay was performed without pyridoxal phosphate supplementation. This facility’s normal ranges of ALT and LDH were 6 to 30 and 119 to 229 U/L, respectively. To focus on the degree of elevation, we set up an index calculated by the following formula: ALT/LDH ratio = (serum ALT − ULN)/(serum LDH − ULN) (ULN: upper limit of normal) as described previously.^{[20 (link)]}

Kuwano A., Okui T., Kohjima M., Kurokawa M., Goya T., Tanaka M., Aoyagi T., Takahashi M., Imoto K., Tashiro S., Suzuki H., Fujita N., Ushijima Y., Ishigami K., Tokunaga S., Kato M, & Ogawa Y. (2023). Transcatheter arterial steroid injection therapy improves the prognosis of patients with acute liver failure. Medicine, 102(10), e33090.

Publication 2023

Biological Assay Enzymes Isoenzymes Lactate Liver Pyridoxal Phosphate Serum Tissues

Optimizing Recombinant Protein Expression

pCold I and pCold TF vectors, as well as restriction endonucleases, were purchased from Takara Corporation (Dalian, China). DNA polymerase and T4 DNA ligase were obtained from Vazyme Biotechnology Corporation (Nanjing, China). The ClonFast kit was acquired from Obio Technology Corporation (Shanghai, China). 2,2′-Dipyridyl, DTT, L-cysteine, L-alanine, L-glutathione reduced (GSH), and deamino-NADH were purchased from Merck (Darmstadt, Germany). Pyridoxal-5′-phosphate was obtained from Sangon Biotechnology Corporation (Shanghai, China). All primers were synthesised by BGI (Shenzhen, China). The remaining chemicals were of analytical grade.

Pang Y., Wang J., Gao X., Jiang M., Zhu L., Liang F., Liang M., Wu X., Xu X., Ren X., Xie T., Wang W., Sun Q., Xiong X., Lyu J., Li J, & Tan G. (2023). Roles of conserved active site residues in the IscS cysteine desulfurase reaction. Frontiers in Microbiology, 14, 1084205.

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Publication 2023

Alanine Cloning Vectors Cysteine DNA-Directed DNA Polymerase DNA Restriction Enzymes nicotinamide-hypoxanthine dinucleotide Oligonucleotide Primers Pyridoxal Phosphate T4 DNA Ligase

Hydrogen Sulfide Measurement in Mouse Brainstem

Anaesthetized mice (urethane, 1.2 g•kg⁻¹i.p.) were rapidly euthanized by decapitation. Following rapid removal of the brainstem, the tissue was flash frozen in liquid N₂. Flash frozen tissues were stored at –80 °C until coronal brainstem sections (300 μm thick) were cut with a cryostat at –20 °C and tissue punches of desired tissue were procured for immediate H₂S measurements. The hypoglossal nucleus and control (inferior olive nucleus) brainstem tissue punches were made from the slices using a chilled micro-punch needle. Hypoglossal tissue from a single brainstem was not sufficient for effectively measuring H₂S levels; therefore, we pooled bilateral micro punched tissue from two mice for each sample where H₂S levels measured. H₂S levels were determined as described previously Yuan et al., 2016 (link). Briefly, cell homogenates from the pooled micro-punch tissue samples were prepared in 100 mM potassium phosphate buffer (pH 7.4). The enzyme reaction was carried out in sealed tubes. The assay mixture in a total volume of 500 μL contained (in final concentration): 100 mM potassium phosphate buffer (pH 7.4), 800 μM l-cysteine, 80 μM pyridoxal 5′-phosphate with or without L-PAG (20 µM) and cell homogenate (20 μg of protein), was incubated at 37 °C for 1 hr. At the end of the reaction, alkaline zinc acetate (1% mass / volume; 250 μL) and trichloroacetic acid (10% vol/vol) were sequentially added to trap H₂S and stop the reaction, respectively. The zinc sulfide formed was reacted with acidic N,N-dimethyl-p-phenylenediamine sulfate (20 μM) and ferric chloride (30 μM) and the absorbance was measured at 670 nm using Shimadzu UV-VIS Spectrophotometer. L-PAG inhibitable H₂S concentration was calculated from a standard curve and values are expressed as nanomoles of H₂S formed per hour per mg of protein.

Browe B.M., Peng Y.J., Nanduri J., Prabhakar N.R, & Garcia AJ I.I.I. (2023). Gasotransmitter modulation of hypoglossal motoneuron activity. eLife, 12, e81978.

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Publication 2023

Acids Biological Assay Brain Stem Buffers Cell Nucleus Cells Cysteine Decapitation dimethyl-4-phenylenediamine Enzymes ferric chloride Freezing Mus Needles Olivary Nucleus potassium phosphate Proteins Pyridoxal Phosphate Sulfates, Inorganic Tissues Trichloroacetic Acid Urethane Zinc Acetate zinc sulfide

Enzyme Catalytic Residue Modification Assay

The involvement of histidine, lysine, tyrosine, and arginine residues in the catalytic action of the enzyme was examined by testing the effect of amino-acid-modifying reagents diethyl pyrocarbonate, pyridoxal 5’-phosphate, 1-acetylimidazole, and phenylglyoxal (Merck, Rahway, NJ, USA), respectively. Stock solution of diethyl pyrocarbonate was prepared by diluting in cold absolute ethanol and quantifying the actual concentration by reaction with 10 mM imidazole (Serva, Heidelberg, Germany) in 0.1 M sodium phosphate, pH 7.3, to form N-carbethoxyimidazole, with a molar absorption coefficient of 3000 M^{- 1}·cm⁻¹ at 230 nm [31 (link)]. The other reagents were dissolved in phosphate buffer. The reactions with enzyme were carried out at 30 °C or at 0 °C in 0.1 M sodium phosphate, pH 7.3. At various times, aliquots were removed and assayed for residual activity. When working with diethyl pyrocarbonate, the inactivation reaction in withdrawn samples was rapidly quenched by twofold dilution with 20 mM imidazole before activity assaying.
To determine the apparent reaction rate constant (k_app) values for enzyme inactivation, a pseudo-first-order kinetics model was used in the form

where k_app is the apparent rate constant, and A(0) and A(t) are the activities at the beginning and after time t of the reaction. For a one-step inactivation mechanism, the apparent rate constant should increase linearly with the initial concentration of inactivator [I]₀:
The slope of the resulting line provides the second-order rate constant (k) for inactivation [32 (link)].
Diethyl pyrocarbonate and 1-acetylimidazole hydrolyze in aqueous solutions. The first-order rate constant k′ for hydrolysis was determined by assaying time courses of changes in concentration in reaction buffer without enzyme. The progress of hydrolysis of diethyl pyrocarbonate was monitored by sampling into imidazole quench solution and measuring the absorbance at 230 nm as described above. The disappearance of 1-acetylimidazole was followed continuously at 243 nm. Taking into account the decomposition of the reagent, the rate equation for loss of enzyme activity is to be modified to [33 (link)]:
Each modification experiment was repeated several times with different concentrations of modifying agent and sampling intervals and the data from a typical experiment are presented.

Kryl M., Sedláček V, & Kučera I. (2023). Structural Insight into Catalysis by the Flavin-Dependent NADH Oxidase (Pden_5119) of Paracoccus denitrificans. International Journal of Molecular Sciences, 24(4), 3732.

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Publication 2023

Amino Acids Arginine Buffers Catalysis Cold Temperature Diethyl Pyrocarbonate enzyme activity Enzymes Ethanol Histidine Hydrolysis imidazole Kinetics Lysine Molar N-acetylimidazole Phenylglyoxal Phosphates Pyridoxal Phosphate sodium phosphate Technique, Dilution Tyrosine

Quantifying Tissue H2S Production Capacity

Measurement of the H₂S production capacity in tissues was performed as previously described.¹⁷ (link)^,²⁷ (link) In brief, 80 μg of protein was incubated in 10 mM L-cysteine and 1 mM pyridoxal 5′-phosphate hydrate (Sigma-Aldrich, St Louis, MO), or 20 μL of plasma was incubated in 100 mM L-cysteine and 10 mM pyridoxal 5′-phosphate hydrate. This mixture was sealed under lead acetate paper and incubated until black lead sulfide precipitate was detected, but not saturated. The lead sulfide presence was quantified using Fiji software, version 1.53f51 (available at: http://fiji.sc/Fiji).

Kiesworo K., MacArthur M.R., Kip P., Agius T., Macabrey D., Lambelet M., Hamard L., Ozaki C.K., Mitchell J.R., Déglise S., Mitchell S.J., Allagnat F, & Longchamp A. (2023). Cystathionine-γ-lyase overexpression modulates oxidized nicotinamide adenine dinucleotide biosynthesis and enhances neovascularization. JVS-Vascular Science, 4, 100095.

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Publication 2023

Cysteine lead acetate lead sulfide Plasma Proteins Pyridoxal Phosphate Tissues

Top products related to «Pyridoxal Phosphate»

Pyridoxal 5 phosphate by Merck Group

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Pyridoxal-5'-phosphate is a coenzyme form of vitamin B6. It serves as a cofactor for various enzymatic reactions in the body, primarily involved in amino acid metabolism.

L cysteine by Merck Group

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L-cysteine is an amino acid that serves as a key component in the manufacturing of various laboratory reagents and equipment. It functions as a building block for proteins and plays a crucial role in the formulation of buffers, cell culture media, and other essential laboratory solutions.

Pyridoxal phosphate by Merck Group

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Pyridoxal phosphate is a coenzyme form of vitamin B6. It is an essential cofactor for various enzymatic reactions in the body, including amino acid metabolism, gluconeogenesis, and neurotransmitter synthesis.

Pyridoxal 5 phosphate hydrate by Merck Group

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Pyridoxal 5'-phosphate hydrate is a chemical compound that serves as a coenzyme in various enzymatic reactions. It is the active form of vitamin B6 and plays a crucial role in protein metabolism, amino acid synthesis, and neurotransmitter production.

Glucose by Merck Group

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Glucose is a laboratory equipment used to measure the concentration of glucose in a sample. It is a fundamental tool in various medical and scientific applications, including the diagnosis and monitoring of diabetes, metabolic research, and food analysis.

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Sodium pyruvate by Merck Group

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Glycine by Merck Group

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Glycine is a colorless, crystalline amino acid that is used as a raw material in the production of various pharmaceutical and chemical products. It serves as a key component in buffer solutions and is commonly employed in the preparation of cell culture media and various biological assays.

What is Pyridoxal Phosphate and why is it important?

Pyridoxal Phosphate is a coenzyme form of vitamin B6 that plays a crucial role in numerous metabolic processes within the body. It serves as a cofactor for various enzymes involved in the metabolism of amino acids, lipids, and carbohydrates. Pyridoxal Phosphate is essential for the proper functioning of the nervous system, the immune system, and the development of red blood cells. Understanding its importance can provide valuable insights into a wide range of physiological and pathological conditions.

What are some common challenges in working with Pyridoxal Phosphate?

One of the main challenges in working with Pyridoxal Phosphate is ensuring reproducibility and accuracy in research protocols. Due to its involvement in multiple metabolic pathways, small variations in experimental conditions can significantly impact the results. Researchers must carefully optimize their protocols to account for factors like sample preparation, assay conditions, and data analysis.

How can PubCompare.ai help with Pyridoxal Phosphate research?

PubCompare.ai's AI-driven platform can assist researchers in optimizing their Pyridoxal Phosphate protocols. The tool allows you to efficiently screen protocol literature, leveraging AI to pinpoint critical insights. PubCompare.ai can help you identify the most effective protocols related to Pyridoxal Phosphate for your specific research goals, highlighting key differences in protocol effectiveness and enabling you to choose the best option for reproducibility and accuaracy.

Are there different forms or variations of Pyridoxal Phosphate?

Yes, there are several forms of Pyridoxal Phosphate, each with its own unique properties and applications. The most common forms include Pyridoxal-5'-Phosphate (PLP), Pyridoxamine-5'-Phosphate (PMP), and Pyridoxine-5'-Phosphate (PNP). These variations can have different roles in enzymatic reactions, cellular signaling, and other physiological processes. Understanding the nuances between these forms is crucial when designing experiments and interpreting results.

More about "Pyridoxal Phosphate"

Pyridoxal-5'-phosphate (PLP) is a crucial coenzyme form of vitamin B6 that plays a vital role in numerous metabolic processes within the human body.
As a cofactor for various enzymes, PLP is essential for the proper functioning of the nervous system, immune system, and the development of red blood cells.
PLP is involved in the metabolism of amino acids, lipids, and carbohydrates, making it a key player in a wide range of physiological and pathological conditions.
Researching the role of PLP in health and disease can provide valuable insights.
Optimizing research protocols for reproducibilty and accuracy is crucial when investigating this important biomolecule.
Leveraging tools like PubCompare.ai's AI-driven platform can help researchers easily locate and compare protocols from literature, preprints, and patents, ensuring they identify the best approach for their PLP-related studies.
PLP, also known as pyridoxal 5'-phosphate or pyridoxal phosphate, is essential for the proper functioning of various enzymes, including those involved in the metabolism of L-cysteine, glucose, ATP, sodium pyruvate, pyruvate, and glycine.
Investigating the interplay between PLP and these related compounds can lead to a deeper understanding of the complex biological processes they influence.
By incorporating synonyms, related terms, and key subtopics, researchers can enhance their PLP-focused studies and unlock new discoveries that contribute to our understanding of this vital coenzyme and its impact on human health and disease.