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Vitamin K2

Most cited protocols related to «Vitamin K2»

Purification and Characterization of Lqo and Mqo

Cited 8 times

C-terminal His₆-tagged versions of Lqo and Mqo were constructed by amplifying alleles from S. aureus strain COL chromosomal DNA using primers Mqo2_His.1A/1B and Mqo1_His.1A/1B, respectively, and cloning into the NcoI/BamHI sites of pQE-60 (Qiagen). Resulting constructs (pJF132 and pJF133) were transformed into E. coli M15 (pREP4; Qiagen) maintained at 37°C with kanamycin (25 μg/ml) and ampicillin (200 μg/ml). For purification, 1 L cultures were seeded with 20 mL overnight cultures, and grown at 25°C for 4 h with selection and the addition of IPTG (0.1 mM). Subsequently, cells were pelleted, washed in PBS and lysed via sonification. Enzymes were purified using HisPur Cobalt Purification System (Pierce) as per manufacturer instruction. Elutions were dialyzed twice for 2 h at 4°C followed by an overnight dialysis at 4°C against high-salt (300 mM NaCl) PBS. Yields were quantified using BCA Protein Quantification Kits (Pierce).
Enzymatic activity for Mqo and Lqo was monitored by addition of 100 ng purified His6-Tagged protein (1 μg if using non-specific substrate) in a 200 μl reaction mixture consisting of 1.4 mM menaquinone, 5 μM flavin adenine dinucleotide (FAD), 643 μg phosphatidylethanolamine (PE), 40 μg NBT and 20 mM substrate (malate/l-lactate). Prior to addition of enzyme, reaction mix was sonicated to uniformly disperse menaquinone within the PE vesicles. Reactions were initiated by addition of substrate and followed via monitoring absorbance at 585 nm using a Tecan infinite M200 plate reader.

Fuller J.R., Vitko N.P., Perkowski E.F., Scott E., Khatri D., Spontak J.S., Thurlow L.R, & Richardson A.R. (2011). Identification of a Lactate-Quinone Oxidoreductase in Staphylococcus aureus that is Essential for Virulence. Frontiers in Cellular and Infection Microbiology, 1, 19.

Publication 2011

Alleles Ampicillin Cells Chromosomes Cobalt Dialysis enzyme activity Enzymes Escherichia coli Flavin-Adenine Dinucleotide Isopropyl Thiogalactoside Kanamycin Lactates M-200 malate menatetrenone Oligonucleotide Primers phosphatidylethanolamine Proteins Sodium Chloride Staphylococcus aureus Strains Synapsin I Vitamin K2

Structural Characterization of VKOR Enzyme

Cited 7 times

The codon-optimized VKOR gene from Synechococcus sp. was expressed with a His tag in E. coli and the protein was purified by Ni- affinity and gel-filtration chromatography in 0.05% DDM. Crystals were obtained by the hanging drop diffusion method and frozen in liquid nitrogen. To obtain heavy atom derivatives, the crystals were soaked with mercury, platinum, or lead compounds. Phases were obtained by the MIR method and improved by solvent flattening. The Trx-like domain (amino acids 186 to 283) was expressed in E. coli, purified, and crystallized. SAD phases were calculated using heavy atom sites found by the direct method, and the model was built and refined automatically. This structure was docked into the density map of the full-length protein. The final model of the full-length protein was manually built and refined to R_work and R_free factors of 24.6% and 30.5%, respectively. The structure factors and coordinates were deposited in the protein data bank (accession code 3KP9 for the full-length protein and accession code 3KP8 for the Trx-like domain).
Disulfide bridge formation in RNAse A was assayed by combining purified VKOR protein (0.5 μM) with reduced, denatured RNAse A (15 μM) and vitamin K 1 quinone (100 μM); the reaction was quenched by addition of 5 × non-reducing SDS buffer supplemented with 50 mM AMS (4-Acetamido-4′-maleimidylstilbene 2,2′-disulfonic acid). Reduction of vitamin K (50 μM) was assayed fluorometrically by excitation at 250 nm and following the emission at 430 nm. The reaction was initiated by addition of either reduced RNAse A (15 μM) or DTT (1 mM). A detailed outline of the experimental procedures is given in Methods.

Li W., Schulman S., Dutton R.J., Boyd D., Beckwith J, & Rapoport T.A. (2010). Structure of a bacterial homolog of vitamin K epoxide reductase. Nature, 463(7280), 507-512.

Publication 2010

Acids Amino Acids Buffers Codon derivatives Diffusion Disulfides Escherichia coli Freezing Gel Chromatography Genes Mercury Nitrogen Platinum Proteins Ribonucleases Solvents Synechococcus Vitamin K Vitamin K2

Vitamin K Content in Dairy Products

Cited 3 times

Fifty of the dairy samples used in this study were provided by USDA Nutrient Data Laboratory, which conducts the National Food and Nutrition Analysis Program (15 ). The nationally collected dairy samples were first delivered to the Food Analysis Laboratory Control Center at Virginia Tech in Blacksburg, Virginia, for preparation of aliquots, and then delivered frozen on dry ice to the Vitamin K Laboratory at Tufts University and stored at −80°C until analysis. The National Food and Nutrition Analysis Program infrastructure incorporates a nationally representative sampling approach (15 , 16 ), approved analytical methods, and a rigorous quality assurance scheme. In addition, 148 dairy samples used in this study were purchased in 2016 from retail outlets that have substantial annual sales in order to capture the diversity of products available in the Boston (Massachusetts) area. Appropriate containers were used to maintain refrigeration during the transport to the laboratory. All of the samples collected by our laboratory were composited, placed in aliquots, and stored at −80°C before analysis. Shelf-life date, analysis date, brand name, and fat content were recorded. We used available information from the manufacturers to determine fat content (i.e., full-fat, reduced-fat, etc.).
The dairy products were grouped in categories on the basis of dairy type and fat content (Table 1): milk, yogurts, Greek yogurts, kefirs, creams, processed cheeses, fresh cheeses, blue cheeses, soft cheeses, semi-soft cheeses, and hard cheeses. Aside from processed cheese, all other types of cheeses included ≥2 different brands and different lots.
All of the cheese sample aliquots (∼10 g) were frozen by liquid nitrogen and manually ground into a powder by using a mortar and pestle. Approximately 0.05–0.2 g of each sample was used for analysis. The procedures for vitamin K extraction and sample purification have been previously described (14 ). Phylloquinone and MK4–13 concentrations were measured by LC-MS by using deuterium-labeled phylloquinone as an internal standard (Sigma Aldrich) and synthesized phylloquinone and MK4–MK13 as calibration standards (14 ).
The effects of dairy product fat content (full-fat, fat-free, or reduced-fat) on concentrations of total vitamin K, phylloquinone, and all detectable menaquinones were analyzed by 2-sample t test. Given the smaller sample size, the vitamin K content of cream products (heavy or whipping cream, half-and-half, and light cream) was examined by general linear model, with heavy or whipping cream used as the reference group. Significance was determined at P < 0.05, and all analyses were carried out by using SAS version 9.4 (SAS Institute). Data are reported as means ± SEMs.

Fu X., Harshman S.G., Shen X., Haytowitz D.B., Karl J.P., Wolfe B.E, & Booth S.L. (2017). Multiple Vitamin K Forms Exist in Dairy Foods. Current Developments in Nutrition, 1(6), e000638.

Publication 2017

Cheese Dairy Products Deuterium Dry Ice Food Food Analysis Freezing Light Milk, Cow's Muscle Rigidity Nitrogen Nutrients Powder Specimen Collection Vitamin K Vitamin K1 Vitamin K2 Yogurt

Anaerobic and Aerobic Growth of Lactobacillus casei

Cited 3 times

The growth of L. casei N87 was evaluated for 24 h at 37°C in modified WMB (10 g/l glucose, without sodium acetate and sodium citrate; mWMB) in batch cultivations carried out under anaerobic (nitrogen flow at 0.1 vol/vol/min; AN), aerobic (30% or 60% dissolved oxygen concentration, DO; AE30 or AE60, respectively) and respiratory (supplementation of mWMB with 2.5 μg/ml hemin and 1 μg/ml menaquinone; with 30% or 60% of DO; RS30 or RS60, respectively) conditions.
Bioreactors (3 l working volume; Applikon, Schiedam, the Netherlands) were inoculated (1% v/v) with an overnight (16 h, 37°C) WMB anaerobic pre-culture, washed twice in 20 mM potassium phosphate buffer pH 7 (PB7). DO was measured using a polarographic electrode (Applisens, Applikon) and was automatically controlled (ezControl controller, Applikon; set point 30% or 60%) by varying the stirrer speed (impeller speed from 200 to 800 rpm; two Rushton turbines, 45 mm diameter) and the opening (from 0% to 100%) of air flow valve (1 vol/vol/min maximum air flow). pH was controlled (pH 6.5) by automatic addition of sterile 4 eq/l NaOH, while foaming was controlled by automatic addition of a sterile 5% (v/v) Antifoam A solution.
Two independent cultivations were carried out for each growth condition (AN, AE30, AE60, RS30, RS60).

Ianniello R.G., Zotta T., Matera A., Genovese F., Parente E, & Ricciardi A. (2016). Investigation of Factors Affecting Aerobic and Respiratory Growth in the Oxygen-Tolerant Strain Lactobacillus casei N87. PLoS ONE, 11(11), e0164065.

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Publication 2016

Bacteria, Aerobic Bioreactors Buffers Glucose Growth Disorders Hemin Nitrogen Oxygen Polarography potassium phosphate Respiratory Rate Sodium Acetate Sodium Citrate Sterility, Reproductive Vitamin K2

Catalase-like Activity in L. casei

Cited 3 times

Since only 4 strains of L. casei (CI4368 from cheese and N87, N811, N2014 from human faeces; Table 1) tolerated 2 mM of H₂O₂ and showed catalase-like activity, a further test was performed to confirm the presence of enzymatic activity and evaluated the effect of oxygen and heme/menaquinone supplementation on tolerance of H₂O₂.
AN, AE and RS cell suspensions (final OD₆₅₀ = 1.0) were exposed (30 min, 37°C) to serial dilutions of H₂O₂ (ten two-fold dilutions from 880 to 1.7 mM). The survivors (if any) were cultivated in microplates as described before. Change of colour from purple to yellow and turbidity were considered as indication of the presence of survivors. Catalase-like activity was measured on the AN, AE and RS cell free extracts (obtained by mechanical lysis in FastPrep-24 Instrument, MP Biomedicals, Santa Ana, California, USA; 5 cycles of 60 sec at speed 6.0) according to the modified protocol of Risse et al. [27] . Briefly, AN, AE and RS samples were first incubated (15 min, 37°C) with 16 mM H₂O₂ (final concentration) and successively (10 min, 37°C) with a mixture containing 4-amino-antipyrine (3 mmol/L), sodium 3,5-dichloro-2 hydroxybenzenesulfonate (10 mmol/L) and peroxidase (0.28 U/mL). The residual amounts of H₂O₂ were spectrophotometrically measured at 510 nm. One µkatal (µkat) was defined as the amount of enzyme required to degrade 1 µmol H₂O₂/s. All measurements were run in duplicate.

Zotta T., Ricciardi A., Ianniello R.G., Parente E., Reale A., Rossi F., Iacumin L., Comi G, & Coppola R. (2014). Assessment of Aerobic and Respiratory Growth in the Lactobacillus casei Group. PLoS ONE, 9(6), e99189.

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Publication 2014

Antipyrine Catalase Cell Extracts Cells Cheese enzyme activity Enzymes Feces Heme Homo sapiens Immune Tolerance Oxygen Peroxidase Peroxide, Hydrogen Sodium Strains Survivors Technique, Dilution Vitamin K2

Most recents protocols related to «Vitamin K2»

Chemotaxonomic Analysis of Bacterial Strains

For the biomass of chemotaxonomic assays, all the tested strains were harvested from BHI-1% NaCl plates after 5 days of incubation at 28°C. Cellular fatty acids were extracted, methylated, and identified by using the Sherlock Microbial Identification System (MIDI) according to the manufacturer’s standard protocols (Sasser, 1990 ). The respiratory isoprenoid quinones were extracted, purified, and analyzed by high performance liquid chromatography (HPLC) (Komagata and Suzuki, 1988 (link)) with various menaquinones and ubiquinones (Hu et al., 2001 (link)) as references. Polar lipids were analyzed using two-dimensional thin-layer chromatography (2D TLC) after hydrolysis with 6 M HCl at 100°C for 18 hours (Staneck and Roberts, 1974 (link); Harper and Davis, 1979 (link)). Peptidoglycan amino acid composition was measured with a Hitachi-8900 high speed amino acid analyzer after hydrolyzing the cell wall, and whole-cell sugars were examined according to the method of Hasegawa et al. (Hasegawa et al., 1983 (link)).
Bacterial carotenoid extracts were analyzed at 450 nm using an UPLC system with DAD detector (UPLC, U3000; Thermo Scientific). The analytical conditions were as follows, UPLC: column, YMC Carotenoid S-3 μm (150 × 4.6 mm); column temperature, 40°C; flow rate, 1.0 mL/min; injection volume, 2 μL; solvent system (MeOH: MTBE: H₂O=20: 75: 5); gradient program, 100:0 v/v at 0 min, 39:61 v/v at 15 min, 0:100 V/V at 25 min, 100:0 v/v at 25.1min, 100:0 v/v at 30 min. Data were acquired on the U3000 UPLC (Thermo Scientific) and processed using chromeleon 7.2 CDS (Thermo Scientific) (Meléndez-Martínez et al., 2010 (link); Irakli et al., 2011 (link)). The carotenoid content in samples was calculated as the formulas: Carotenoid content (µg/100 mL) = Read concentration (µg/mL) × Dilution factor × 100.

Huang Y., Zhang S., Tao Y., Yang J., Lu S., Jin D., Pu J., Luo W., Zheng H., Liu L., Jiang J.F, & Xu J. (2023). Morphological and genomic characteristics of two novel actinomycetes, Ornithinimicrobium sufpigmenti sp. nov. and Ornithinimicrobium faecis sp. nov. isolated from bat faeces (Rousettus leschenaultia and Taphozous perforates). Frontiers in Cellular and Infection Microbiology, 13, 1093407.

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Publication 2023

Amino Acids Bacteria Biological Assay Carotenoids Cells Cell Wall Diet, Formula Fatty Acids High-Performance Liquid Chromatographies Hydrolysis Isoprenoids Lipids methyl tert-butyl ether Peptidoglycan Quinones Respiratory Rate Sodium Chloride Solvents Strains Sugars Technique, Dilution Thin Layer Chromatography ubidecarenone Vitamin K2

Quantification of Liver Vitamin K Levels

The levels of vitamin K in the liver were measured in the microsomal fraction using the Sherman and Sander method (1981) [28 (link)]. To obtain the microsomal fraction, the liver was homogenized in a sucrose buffer 0.25 M (pH 7.5) (ratio 1:4 g/mL) using a Tissue grinder (Ultra-Turrax^® T25 basic IKA, Saint Louis, MS, USA) at 4 °C. The homogenate was centrifuged at 9000× g for 20 min and the supernatant was discarded. The pellet was centrifuged again at 100,000× g for 60 min. The supernatant was discarded again, and the resulting pellet was resuspended with KCl buffer 1.15% at pH 7.5 (ratio 1:2.6 g/mL) and then re-homogenized. A liquid solution of vitamin K epoxide (10 µL of vitamin K epoxide in methanol 95%) was added to 500 µL of microsomes, giving a final concentration of 10 µM. Then 1 mL of isopropanol/hexane (3:2) was added to the mixture and centrifuged at 9000× g for 5 min. An aliquot of 300 µL of the upper hexane phase was removed from the mixture and the remainder was left to evaporate at room temperature. The sample was diluted in 100 µL of isopropanol and stirred for 20 min. Finally, 20 µL were taken and then analyzed with HPLC. Three replicates were performed for each sample. The HPLC method was optimized following the Jakob and Elmadfa (1996) [29 (link)] method. The analysis was carried out with an RP-C18 column (SUPELCO Kromasil 100A-5u-C18 4.6 mm × 250 mm), at a flow rate of 1 mL/min and the absorbance set at 254 nm. The total run time was 15 min. The mobile phase consisted of methanol/dichloromethane 75/25% (v/v) maintained in isocratic conditions. An external standard calibration curve consisting of six points at the increasing concentrations of 1, 5, 10, 50, 150, and 300 μg per mL was prepared using the standard solution of vitamin K and vitamin K 2, 3-epoxide (vitamin K and vitamin K 2,3-epoxide LOD = 0.01 µg/mL; LOQ = 0.01 µg/mL) (Figure S1).

Caliani I., Di Noi A., Amico C., Berni R., Romi M., Cai G., Guarnieri M., Navone A., Spano G., Howald G.R., Sposimo P, & Marsili L. (2023). Brodifacoum Levels and Biomarkers in Coastal Fish Species following a Rodent Eradication in an Italian Marine Protected Area: Preliminary Results. Life, 13(2), 415.

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Publication 2023

Buffers Epoxy Compounds High-Performance Liquid Chromatographies Isopropyl Alcohol Liver Methanol Methylene Chloride Microsomes n-hexane Sucrose Tissues Vitamin K vitamin K1 oxide Vitamin K2

Coagulation Factor and Anticoagulant Assay

Dichloromethane, acetone, methanol, acetonitrile, sucrose buffer, KCl buffer, isopropanol, hexane, and Giemsa stain were purchased from Sigma-Aldrich, St. Louis, MO, USA. Standard solutions of brodifacoum, vitamin K, and vitamin K 2,3-epoxide were also purchased from Sigma-Aldrich, St. Louis, MO, USA. The ReadiPlasTin kit (HemosiIL) was purchased from Werfen, Milan, Italy.

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Publication 2023

Acetone acetonitrile bromfenacoum Buffers Epoxy Compounds Isopropyl Alcohol Methanol Methylene Chloride n-hexane Stain, Giemsa Sucrose Vitamin K Vitamin K2

Atorvastatin + Dietary Supplement in Hypercholesterolemia

A randomized, double-blind, placebo-controlled parallel-groups study was conducted following the guidelines laid down in the Declaration of Helsinki. The trial procedure was approved by the ethics committee of University Clinical Centre Zvezdara, Belgrade, Serbia. Written consent from all participants was obtained before initiating the study. The trial was registered at Australian New Zealand Clinical Trials Registry (ACTRN12619000102178; http://www.anzctr.org.au).
One-hundred and seventy-seven outpatients from the Department of Cardiology, University Clinical Centre Zvezdara, Belgrade, Serbia were initially screened for eligibility. Finally, eighty-seven men and women, aged 40–80 years, were recruited for this 13-week study. All patients had a diagnosis of hypercholesterolemia or mixed dyslipidaemia with a minimum four-month using atorvastatin (20 mg/day) prior to study. The power calculation has been done before the study and was described in detail in our previous report [32] (link). Patients with acute coronary syndrome(within the previous month), serious heart failure, renal dysfunction, liver disorders, cerebral vascular disease or mental illness were excluded from the study. None of the participants used substances or practiced habits known to act pro-oxidative or affect anti-oxidative defense system. During 13 weeks of intervention period, participants did not change their individual dietary habits and preferences. Participants were randomly assigned to receive either atorvastatin 20 mg/d + placebo (n = 45) or atorvastatin 20 mg/d + dietary supplement (DS) which contains Octa cosanol (20 mg) and Vitamin K2 (40 μg) (n = 42). All capsules (DS and placebo) were supplied by Abela Pharm d.o.o., Belgrade, Serbia. Placebo capsules were identical to DS capsules in terms of their size, color, shape, and smell. The placebo contained all the ingredients of DS capsules except for the bioactive ingredients. Participants were scheduled for follow-up visits when any unusual adverse effects were reported by using appropriate record forms. To monitor compliance, patients were asked to return any unused capsules.

Zrnić-Ćirić M., Kotur-Stevuljević J., Stanković I., Đordjević B., Baralić I, & Ostojić M. (2023). Association of octacosanol supplementation with redox status in patients on chronic statin therapy. Journal of Medical Biochemistry, 42(1), 47-57.

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Publication 2023

Acute Coronary Syndrome Atorvastatin Capsule Cardiovascular System Cerebrovascular Disorders Congestive Heart Failure Diagnosis Dietary Supplements Dyslipidemias Eligibility Determination Ethics Committees, Clinical Hypercholesterolemia Kidney Failure Liver Diseases Mental Disorders Outpatients Patients Placebos Sense of Smell Vitamin K2 Woman

Osteoporosis Treatment Strategies

All morbid states during observation as well as at baseline were properly treated over the follow-up period after obtaining informed consent from the participants. All subjects with osteoporosis were asked for receiving osteoporotic treatment. When the patients agreed with treatment, the patients themselves selected the modes of treatment with the advice from clinicians. Definition of the treatment was as follows. The mode of treatment included teriparatide, estrogen, selective estrogen receptor modulators (SERMs), bisphosphonates, or denosumab. When the treatment term exceeded half of the observation period, we defined those subjects as the patients with treatment. Vitamin D analogue, vitamin K2, calcium formulation, or calcitonin were not included in the treatment because of the lack of robust data for preventing fractures. Randomization of the treatment mode was impossible, because the treatment procedure depended upon the patient’s will. The treatment of osteoporosis was basically not changed until the occurrence of incident fracture or adverse event. Thus, the duration of treatment was the same as observation period in nearly all cases.

Shiraki M., Kuroda T., Nakano M., Nakamura Y., Saito M, & Urano T. (2023). Nitric oxide is associated with fracture risk in Japanese women. PLOS ONE, 18(2), e0280854.

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Publication 2023

Calcitonin Calcium Denosumab Diphosphonates Estrogens Fracture, Bone Osteoporosis Patients Selective Estrogen Receptor Modulators Teriparatide Vitamin D Vitamin K2

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Vitamin k1 by Merck Group

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Fluorescence microscope by Olympus

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More about "Vitamin K2"

Vitamin K2, also known as menaquinone, is an essential nutrient that plays a crucial role in blood coagulation and bone health.
It is involved in the activation of certain proteins that regulate calcium deposition in the body.
This fat-soluble vitamin can be found in a variety of fermented foods, such as natto, as well as in some dairy products and meat.
Research suggests that supplementation with Vitamin K2 may help to improve bone density and reduce the risk of cardiovascular disease.
The TC-C18 column is often used for the chromatographic separation and analysis of Vitamin K2 and its related compounds.
Vitamin K1, also known as phylloquinone, is another form of vitamin K that is primarily found in green leafy vegetables.
Triton X-100 is a non-ionic surfactant that is sometimes used in the extraction and purification of Vitamin K2 from biological samples.
Fluorescence microscopy can be a useful technique for visualizing the cellular localization and distribution of Vitamin K2 within living cells.
Lipofectamine 2000 is a transfection reagent that can be used to introduce Vitamin K2 or related genes into cultured cells.
Isopropanol and acetonitrile are common solvents used in the extraction and analysis of Vitamin K2 from various matrices.
DMSO (dimethyl sulfoxide) is another solvent that can be used in Vitamin K2 research, particularly in cell culture experiments.
Horse heart cytochrome c is sometimes used as a reference standard in Vitamin K2 analysis.
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