Only in Titles

Search results for: Purified

paperclip

#33091674   2020/10/06 To Up

Simple and fast UPLC-MS method for quantifying the anti-inflammatory candidate 5'-methoxynobiletin in rat plasma: Validation and application in a preliminary pharmacokinetic study.

This study presents the development and validation of a fast and simple bioanalytical ultra-performance liquid chromatography-tandem mass spectrometry (UPLC-MS) method intended for quantifying the anti-inflammatory candidate 5'-methoxynobiletin (5'-MeONB) in rat plasma. Standard of 5'-MeONB was purified from A. conyzoides extract by using preparative HPLC. After a pretreatment of plasma samples with acetonitrile, chromatographic separations were efficiently achieved with a C column using a 9 min gradient system of 0.1% aqueous formic acid and acetonitrile as eluent. Drug candidate 5'-MeONB and chrysin (internal standard, IS) detection were carried out using ESI+ through the extracted ion chromatograms approach, monitored at m/z 433.1494 (for 5'-MeONB, t:1.78 min) and m/z 255.0657 (for IS, t:1.57 min). Method was validated according to US FDA guidelines, presenting linearity (R > 0.999) over concentration range of 30-750 ng/mL. Relative standard deviation (RSD) of repeatability and intermediary precision respectively ranged between 1.93-3.65% and 2.16-7.54%, considering lower limit of quantitation (30 ng/mL) and quality control (90, 360 and 600 ng/mL) samples, while accuracy was between 82.51 and 109.44%. Moreover, no interference from plasma endogenous substances, no carryover effect, and no influence of extraction method even in hemolyzed blood samples were observed. Sample stability in auto-sampler and long-term -80 °C storage, as well as matrix effect were within acceptable limits. For the first time, using the validated UPLC-MS bioanalytical method, the plasma pharmacokinetics of 5'-MeONB following 2 mg/kg intravenous bolus dosing to Wistar rats was characterized allowing the determination of the parameters describing drug distribution and elimination.
Larissa Gabriela Faqueti, Layzon Antonio Lemos da Silva, Gabriela Salim Gomes Moreira, Luciana Aparecida Honorato, Adair Roberto Soares Dos Santos, Teresa Dalla Costa, Maique Weber Biavatti

1296 related Products with: Simple and fast UPLC-MS method for quantifying the anti-inflammatory candidate 5'-methoxynobiletin in rat plasma: Validation and application in a preliminary pharmacokinetic study.

100ug Lyophilized0.1ml100ug Lyophilized0.1ml100ug Lyophilized100ug Lyophilized0.1ml100ug Lyophilized0.1ml

Related Pathways

paperclip

#33091476   2020/10/19 To Up

Improved production of an acidic exopolysaccharide, the efficient flocculant, by Lipomyces starkeyi U9 overexpressing UDP-glucose dehydrogenase gene.

In order to increase content of glucuronic acid in the exopolysaccharide (EPS) and its flocculating activity, an UDP-glucose dehydrogenase gene was overexpressed in Lipomyces starkeyi V19. The obtained U9 strain could produce 62.1 ± 1.2 g/l EPS while the V19 strain only produced 53.5 ± 1.3 g/l EPS. The compositions of monosaccharides in the purified EPS (U9-EPS) from the U9 strain contained 3.79:1:5.52 while those in the purified EPS (V19-EPS) were 3.94:1:6.29. The flocculation rate of the U9-EPS on kaolin clay reached 87.9%, which was significantly higher than that (74.7%) of the V19-EPS while the decolorization rate of Congo Red (CR) by the U9-EPS reached 94.3%, which was significantly higher than that of CR by the V19-EPS (86.23%). The results showed that the purified bioflocculant U9-EPS had effective flocculation of kaolin clay. The U9-EPS also had high ability to flocculate the polluted river water and decolorize Congo red.
Xin Yu, Xin Wei, Zhe Chi, Guang-Lei Liu, Zhong Hu, Zhen-Ming Chi

1393 related Products with: Improved production of an acidic exopolysaccharide, the efficient flocculant, by Lipomyces starkeyi U9 overexpressing UDP-glucose dehydrogenase gene.

100ug Lyophilized100ug Lyophilized100ug100 μg100ug1 ml100ug Lyophilized100 200 200ul

Related Pathways

paperclip

#33091044   2020/10/22 To Up

Effective refolding of a cysteine rich glycoside hydrolase family 19 recombinant chitinase from Streptomyces griseus by reverse dilution and affinity chromatography.

Conventional refolding methods are associated with low yields due to misfolding and high aggregation rates or very dilute proteins. In this study, we describe the optimization of the conventional methods of reverse dilution and affinity chromatography for obtaining high yields of a cysteine rich recombinant glycoside hydrolase family 19 chitinase from Streptomyces griseus HUT6037 (SgChiC). SgChiC is a potential biocontrol agent and a reference enzyme in the study and development of chitinases for various applications. The overexpression of SgChiC was previously achieved by periplasmic localization from where it was extracted by osmotic shock and then purified by hydroxyapatite column chromatography. In the present study, the successful refolding and recovery of recombinant SgChiC (r-SgChiC) from inclusion bodies (IB) by reverse dilution and column chromatography methods is respectively described. Approximately 8 mg of r-SgChiC was obtained from each method with specific activities of 28 and 52 U/mg respectively. These yields are comparable to that obtained from a 1 L culture volume of the same protein isolated from the periplasmic space of E. coli BL21 (DE3) as described in previous studies. The higher yields obtained are attributed to the successful suppression of aggregation by a stepwise reduction of denaturant from high, to intermediate, and finally to low concentrations. These methods are straight forward, requiring the use of fewer refolding agents compared with previously described refolding methods. They can be applied to the refolding of other cysteine rich proteins expressed as inclusion bodies to obtain high yields of actively folded proteins. This is the first report on the recovery of actively folded SgChiC from inclusion bodies.
Ayokunmi Omolola Oyeleye, Siti Faridah Mohd Yusoff, Izzah Nadiah Abd Rahim, Adam Thean Chor Leow, Noor Baity Saidi, Yahaya M Normi

1858 related Products with: Effective refolding of a cysteine rich glycoside hydrolase family 19 recombinant chitinase from Streptomyces griseus by reverse dilution and affinity chromatography.

100ul100 µg100 µg100.00 ug1 mg5 mg5 mg200ul25 100ug Lyophilized2100ug Lyophilized

Related Pathways

paperclip

#33090589   2020/10/08 To Up

Characterization of xanthine oxidase from Cellulosimicrobium funkei possessing hypoxanthine-metabolizing activity.

Purine-degrading enzymes are favorable as medications and diagnostic tools for hyperuricemia. This study aimed to characterize enzymes isolated from microorganisms, which may useful for developing a new prophylaxis for hyperuricemia.
Iori Kozono, Michiki Takeuchi, Shoko Kozono, Atsushi Satomura, Wataru Aoki, Makoto Hibi, Jun Ogawa

2211 related Products with: Characterization of xanthine oxidase from Cellulosimicrobium funkei possessing hypoxanthine-metabolizing activity.

100 assays1 kit50 mg100 tests 100ul100 assays100 assays1 kit100 assays2.5 mg 96 Tests

Related Pathways

paperclip

#33089605   2020/10/22 To Up

Comment on "An observational pilot study using a purified reconstituted bilayer matrix to treat non-healing diabetic foot ulcers".


Adam L Isaac, Michael Tritto

2403 related Products with: Comment on "An observational pilot study using a purified reconstituted bilayer matrix to treat non-healing diabetic foot ulcers".

200ug100 µg0.1mg1 module100 mg100μg100μl100μl250ug100μl100μl100μl

Related Pathways

    No related Items
paperclip

#33089232   2020/09/30 To Up

Exploring the feasibility of Typhimurium-specific phage as a novel bio-receptor.

The purpose of this study was aimed to isolate a Typhimurium-specific phage (KFS-ST) from washing water in a poultry processing facility and to investigate the feasibility of the KFS-ST as a novel bio-receptor for the magnetoelastic (ME) biosensor method. KFS-ST against . Typhimurium was isolated, propagated, and purified using a CsCl-gradient ultracentrifugation. Morphological characteristics of KFS-ST were analyzed using transmission electron microscopy (TEM). Its specificity and efficiency of plating analysis were conducted against 39 foodborne pathogens. The temperature and pH stabilities of KFS-ST were investigated by the exposure of the phage to various temperatures (-70°C-70°C) and pHs (1-12) for 1 h. A one-step growth curve analysis was performed to determine the eclipse time, latent time and burst size of phage. The storage stability of KFS-ST was studied by exposing KFS-ST to various storage temperatures (-70°C, -20°C, 4°C, and 22°C) for 12 weeks. KFS-ST was isolated and purified with a high concentration of (11.47 ± 0.25) Log PFU/mL. It had an icosahedral head (56.91 ± 2.90 nm) and a non-contractile tail (225.49 ± 2.67 nm), which was classified into the family of in the order of . KFS-ST exhibited an excellent specificity against only Typhimurium and . Enteritidis, which are considered two of the most problematic strains in the meat and poultry. However, KFS-ST did not exhibit any specificity against six other and 27 non- strains. KFS-ST was stable at temperature of 4°C to 50°C and at pH of 4 to 12. The eclipse time, latent time, and burst size of KFS-ST were determined to be 10 min, 25 min and 26 PFU/ infected cell, respectively. KFS-ST was relatively stable during the 12-week storage period at all tested temperatures. Therefore, this study demonstrated the feasibility of KFS-ST as a novel bio-receptor for the detection of Typhimurium and Enteritidis in meat and poultry products using the ME biosensor method.
In Young Choi, Do Hyeon Park, Brayan A Chin, Cheonghoon Lee, Jinyoung Lee, Mi-Kyung Park

1312 related Products with: Exploring the feasibility of Typhimurium-specific phage as a novel bio-receptor.

2 Pieces/Box2 Pieces/Box2 Pieces/Box100 assays1 kit100 assays100 ug/vial100ug100ug1000 assays

Related Pathways

paperclip

#33088938   2020/10/14 To Up

Phylogenetic analysis and epidemiological history of Hepatitis E virus 3f and 3c in swine and wild boar, Italy.

Hepatitis E virus (HEV) genotype 3 has a worldwide distribution. The food-borne transmission of HEV associated with the consumption of products derived from domestic pig, wild boar has been reported in various countries. In this study the genetic diversity, evolutionary rates of HEV 3f, 3c among swine and wild boar in Italy were estimated.
Alessandra Lo Presti, Roberto Bruni, Umbertina Villano, Cinzia Marcantonio, Michele Equestre, Massimo Ciuffetelli, Alessandro Grimaldi, Elisabetta Suffredini, Simona Di Pasquale, Dario De Medici, Anna Rita Ciccaglione

1554 related Products with: Phylogenetic analysis and epidemiological history of Hepatitis E virus 3f and 3c in swine and wild boar, Italy.

96T 5 G96 wells (1 kit)10 mg200ug500 MG25 mg100ug100ul100ug0.1 mg50 mg

Related Pathways

paperclip

#33088656   2020/09/30 To Up

Purification and biochemical characterization of an extracellular fructosyltransferase enzyme from sp. XOBP48: implication in fructooligosaccharide production.

An extracellular fructosyltransferase (Ftase) enzyme with a molar mass of ≈70 kDa from a newly isolated indigenous coprophilous fungus sp. XOBP48 is purified to homogeneity and characterized in this study. The enzyme was purified to 4.66-fold with a total yield of 15.53% and specific activity of 1219.17 U mg of protein after a three-step procedure involving (NH)SO fractionation, dialysis and anion exchange chromatography. Ftase showed optimum activity at pH 6.0 and temperature 50 °C. Ftase exhibited over 80% residual activity at pH range of 4.0-10.0 and ≈90% residual activity at temperature range of 40-60 °C for 6 h. Metal ion inhibitors Hg and Ag significantly inhibited Ftase activity at 1 mmol concentration. Ftase showed , and values of 79.51 mmol, 45.04 µmol min and 31.5 min, respectively, with a catalytic efficiency (/) of 396 µmol min for the substrate sucrose. HPLC-RI experiments identified the end products of fructosyltransferase activity as monomeric glucose, 1-kestose (GF), and 1,1-kestotetraose (GF). This study evaluates the feasibility of using this purified extracellular Ftase for the enzymatic synthesis of biofunctional fructooligosaccharides.
Jeff Ojwach, Ajit Kumar, Samson Mukaratirwa, Taurai Mutanda

1779 related Products with: Purification and biochemical characterization of an extracellular fructosyltransferase enzyme from sp. XOBP48: implication in fructooligosaccharide production.

900 tests100ug100ug100 μg100ug100 μg100 μg100 μg100ug Lyophilized1 Set1 Set100 μg

Related Pathways

paperclip

Error loading info... Pleas try again later.
paperclip

Error loading info... Pleas try again later.