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#23451505   2013/03/04 Save this To Up

[Study on the flax seed enzymatic degumming process by central composite design and response surface method].

To optimize extraction condition of degumming from flax seed by the response surface method.

1801 related Products with: [Study on the flax seed enzymatic degumming process by central composite design and response surface method].

Anti beta3 AR Human, Poly CAR,CAR,Constitutive acti Bcl-2 Oncoprotein; Clone Bcl-2 Oncoprotein; Clone c-erbB-2 Oncoprotein c-erbB-2 Oncoprotein c-erbB-3 Oncoprotein; Cl c-erbB-3 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl

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#20599493   2010/08/31 Save this To Up

Formulation and stability of a novel artificial human sweat under conditions of storage and use.

A limitation of most artificial sweat formulations used for in vitro assessment of chemical release from materials in contact with skin have little biological relevance to human sweat. The purposes of this paper are to provide guidance for preparation of a novel artificial sweat with chemical constituents at concentrations that match human sweat and to characterize chemical stability. The artificial sweat was characterized under conditions of use (with and without sebum at 36 degrees C) and storage (without sebum at -4, 4, and 23 degrees C) over 28 days by gas chromatography-mass spectroscopy, high-performance liquid chromatography, enzymatic assay kits, and ion-selective electrodes. Seven indicator constituents were tracked: sodium, chloride, glucose, lactic acid, urea, pantothenic acid, and alanine. With or without sebum at 36 degrees C, the sweat solvent was chemically stable for 14 days. Storage by refrigeration at 4 degrees C retained the chemical integrity of the solvent longest. Based on these results, the solvent should be used within 14 days of preparation. The artificial sweat model presented herein is most similar to human sweat and has applications as a dissolution solvent, donor solution in diffusion cells, or vehicle for patch testing. This sweat model may aid researchers in understanding potential release and percutaneous absorption of chemicals in contact with human skin surface liquids.

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Rabbit Anti-Human Androge Rabbit Anti-Human Androge Rabbit Anti-Human Androge Goat Anti-Human Androgen CAR,CAR,Constitutive acti Recombinant Human Androge Androgen Receptor (Phosph Androgen Receptor (Phosph Androgen Receptor (Ab 650 AZD-3514 Mechanisms: Andr 17β-Acetoxy-2α-bromo-5 (5α,16β)-N-Acetyl-16-[2

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#19484410   2010/02/10 Save this To Up

Purification and partial characterization of an exo-polygalacturonase from Paecilomyces variotii liquid cultures.

An extracellular polygalacturonase (PG) produced from Paecilomyces variotii was purified to homogeneity through two chromatography steps using DEAE-Fractogel and Sephadex G-100. The molecular weight of P. variotii PG was 77,300 Da by gel filtration and SDS-PAGE. PG had isoelectric point of 4.37 and optimum pH 4.0. PG was very stable from pH 3.0 to 6.0. The extent of hydrolysis of different pectins by the purified enzyme was decreased with an increase in the degree of esterification. PG had no activity toward non-pectic polysaccharides. The apparent K(m) and V(max) values for hydrolyzing sodium polypectate were 1.84 mg/mL and 432 micromol/min/mg, respectively. PG was found to have temperature optimum at 65 degrees Celsius and was totally stable at 45 degrees Celsius for 90 min. Half-life at 55 degrees Celsius was 50.6 min. Almost all the examined metal cations showed partial inhibitory effects under enzymatic activity, except for Na(+1), K(+1), and Co(+2) (1 mM) and Cu(+2) (1 and 10 mM).

1933 related Products with: Purification and partial characterization of an exo-polygalacturonase from Paecilomyces variotii liquid cultures.

Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650 Annexin V Blocking Peptid Annexin VIII Blocking Pep AZD-3514 Mechanisms: Andr 17β-Acetoxy-2α-bromo-5 (5α,16β)-N-Acetyl-16-[2 (5α,16β)-N-Acetyl-16-ac 5α-N-Acetyl-2'H-androst-

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#16455312   2006/03/07 Save this To Up

Stability of glufosfamide in phosphate buffers and in biological samples.

Glufosfamide is a new, potential chemotherapeutic agent currently under investigation. Stability of glufosfamide was investigated in sodium phosphate buffers with different pH and temperature and in biological samples. Glufosfamide and isophosphamide mustard were quantified simultaneously using a liquid chromatography-ion trap mass spectrometric method; precision and accuracy were within 15% for each analyte. Glufosfamide was stable in neutral buffers, but decomposed to form isophosphoramide mustard under acidic and basic conditions, which was pH- and temperature-dependent. The stability of glufosfamide varied in different biological samples. Results indicated that glufosfamide was unstable in some biological samples, such as the small intestine, smooth muscles, pancreas and urine, especially in the small intestine homogenate, with a half-life of 1.1 h. But the pH (<8) and beta-glucosidase of the tissue homogenate was found to have negligible contribution to the degradation of glufosfamide. The enzymatic inhibition experiment with the specific inhibitor, saccharo-1,4-lactone, demonstrated that it was glucuronidase that resulted in the degradation of glufosfamide in small intestine homogenate. Methanol was recommended to be used to homogenize the tissue in an ice water bath, and the container for urine collection should also be maintained in an ice water bath, and all the biological samples collected should be preserved in frozen condition until analysis.

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Directed In Vivo Angiogen Cultrex 96 Well Laminin I Cultrex 96 Well Collagen Cultrex 96 Well Collagen Cultrex96 Well 3D BME Cel Inflammation (Human) Quan Inflammation (Human) Quan Inflammation (Human) Quan Inflammation (Mouse) Quan Inflammation (Rat) Quanti Homogenizer for 24 sample Bullet Blender 50-DX homo

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#12783196   2003/06/03 Save this To Up

Enzymatic dehalogenation of pentachlorophenol by Pseudomonas fluorescens of the microbial community from tannery effluent.

Four different bacterial isolates obtained from a stable bacterial consortium were capable of utilizing pentachlorophenol (PCP) as sole carbon and energy source. The consortium was developed by continuous enrichment in the chemostat. The degradation of PCP by bacterial strain was preceded through an oxidative route as indicated by accumulation of tetrachloro-rho-hydroquinone and dichlorohydroquinone as determined by high performance liquid chromatography (HPLC). Among the four isolates, Pseudomonas fluorescens exhibited maximum degradation capability and enzyme production. PCP-monooxygenase enzyme was extracted from culture extract and fractionated by DEAE-cellulose ion exchange chromatography. The molecular weight of the enzyme, purified from Pseudomonas fluorescens, determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography was found to be 24000 Da.

2679 related Products with: Enzymatic dehalogenation of pentachlorophenol by Pseudomonas fluorescens of the microbial community from tannery effluent.

Ofloxacin CAS Number [824 BACTERIOLOGY PSEUDOMONAS PSEUDOMONAS AERUGINOSA cl BACTERIOLOGY BACTEROIDES Leupeptin, hemisulfate (M Leupeptin, hemisulfate (M Leupeptin, hemisulfate (M Leupeptin, hemisulfate (M Leupeptin, hemisulfate (M Leupeptin, hemisulfate (M TCP-1 theta antibody Sour Recombinant Thermostable

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#11710100   2001/11/16 Save this To Up

Identification of a marine benthic P(3HB)-degrading bacterium isolate and characterization of its P(3HB) depolymerase.

A poly[(R)-3-hydroxybutyrate] (P(3HB))-degrading marine bacterium (strain NK-1, JCM10458) was isolated from the Pacific Ocean deep-sea floor (1165 m in depth) in Japan. The organism was a motile and Gram negative, aerobic, and rod-shaped bacterium, and its DNA had a guanine-plus-cytosine content of 57.7 mol%. On the basis of several phenotypic characters and a phylogenetic analysis of the gene coding for 16S rRNA, this strain was identified as Marinobacter sp. The strain required sodium salt for growth in the medium and secreted a P(3HB) depolymerase into the supernatant when it was cultivated on (S)-3-hydroxybutyric acid or P(3HB) as the sole carbon source. The P(3HB) depolymerase (PhaZMsp) was purified to homogeneity from the culture supernatant of Marinobacter sp. by hydrophobic and ion exchange column chromatography and showed a molecular mass of 70 kDa. PhaZMsp was stable at temperatures below 37 degrees C and at pH values of 7.5-10.0. The N-terminal amino acid sequences of both the purified enzyme and the truncated one shared high homologies to the N-terminal and internal sequences of Pseudomonas stutzeri depolymerase, respectively. High-performance liquid chromatography analysis revealed that the enzymatic products of P(3HB) yielded monomer, dimer, and trimer of 3-hydroxybutyric acid. PhaZMsp was capable of hydrolyzing P(3HB), poly(3-hydroxypropionate), and poly(4-hydroxybutyrate).

1809 related Products with: Identification of a marine benthic P(3HB)-degrading bacterium isolate and characterization of its P(3HB) depolymerase.

Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon BACTERIOLOGY PSEUDOMONAS PSEUDOMONAS AERUGINOSA cl Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650 anti GFP antibody, rat mo

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#7947705   1994/12/06 Save this To Up

Detergent-solubilized monomeric and dimeric cytochrome bc1 isolated from bovine heart.

Mitochondrial cytochrome bc1 complex, isolated from frozen bovine heart, was solubilized with five different "non-denaturing" detergents: dodecyl maltoside, octaethylene glycol monododecyl ether (C12E8), Triton X-100, Tween 20, and sodium cholate. The hydrodynamic properties of the solubilized complex III's were then investigated by sedimentation analysis. Complex III exists as a stable and monodisperse dimer when it is solubilized in low ionic strength buffer with a low concentration of any of the five detergents. At pH 7.8, 20 degrees C, the protein sediments as a homogeneous species with an s(obs) of about 14 S. The protein molecular weight of the 14S particle, after correction for bound detergent, is 465,000 +/- 30,000 as measured by sedimentation equilibrium analysis. The aggregation state and/or homogeneity of cytochrome bc1 is strongly dependent upon the concentration of the solubilizing detergent and ionic strength. The enzyme becomes a homogeneous, monomeric complex with a protein molecular weight of 235,000 +/- 20,000 and an s(obs) of 10-10.5 S after it is solubilized in high concentrations of Tween 20 (more than 5 mg/mg of protein) and sodium chloride (more than 0.5 M). However, a heterogeneous mixture of subcomplexes is produced upon solubilization of the complex with high concentrations of the other detergents and 0.5 M NaCl. Monomerization of cytochrome bc1 by Tween 20 and 0.5 M NaCl has no effect on either the spectral properties, the subunit composition, or the enzymatic activity and is reversible since the dimeric 14S particle is regenerated upon removal of the high concentration of salt.(ABSTRACT TRUNCATED AT 250 WORDS)

2891 related Products with: Detergent-solubilized monomeric and dimeric cytochrome bc1 isolated from bovine heart.

Bovine Androstenedione,AS Non-sterile bovine plasm Non-sterile bovine plasm Non-sterile bovine serum Non-sterile bovine serum Cytochrome P450 2C9 Cytochrome P450 3A4 MOUSE ANTI BOVINE ROTAVIR Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon

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#2188980   1990/07/02 Save this To Up

Purification and characterization of recombinant plasminogen activator inhibitor-1 from Escherichia coli.

A recombinant form of plasminogen activator inhibitor-1 (rPAI-1) has been purified from lysates of pCE1200, a bacterial expression vector containing the full length PAI-1 gene, by utilizing sequential anion exchange and cation exchange chromatography on Q-Sepharose and S-Sepharose columns. Approximately 140 mg of rPAI-1, estimated at 98% purity on the basis of analytical high performance liquid chromatography, could be obtained from 200 g wet weight of cells. The purified protein exhibited a single Coomassie Blue-stainable band at the region of Mr = 42,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and an NH2-terminal amino acid sequence consistent with the expected translation product of the pCE1200 PAI-1 insert. The rPAI-1 rapidly inhibited single- and two-chain tissue plasminogen activators, as well as urokinase, with apparent second order rate constants in the range of 2-5 x 10(7) M-1 s-1. A specific activity measurement of 250,000 units/mg was calculated for the rPAI-1 based on its ability to inhibit the enzymatic activity of a single-chain tissue plasminogen activator. Stability studies showed that the activity of the rPAI-1 was very stable when stored at temperatures of 25 degrees C or lower, but decayed within hours when stored at 37 degrees C. Sodium dodecyl sulfate treatment, which partially activates the latent form of natural PAI-1, inactivated rPAI-1. These results show that the purified rPAI-1 produced from pCE1200 displays many of the properties associated with the biologically active form of natural PAI-1.

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#3920229   1985/04/26 Save this To Up

Identification of phenols of 7,12-dimethylbenz[a]anthracene by conversion into their methyl ethers.

The compound 7,12-dimethylbenz[a]anthracene (DMBA), a powerful chemical carcinogen, undergoes enzymatic oxidation to a variety of metabolites. Phenols, the monohydroxylated derivatives of DMBA, are an electrophilic species capable of binding covalently with DNA. Although phenols may play a role in carcinogenesis, little information is available regarding these metabolites, many of which are chemically unstable and elusive to quantitative analysis. In this study, a method is described for the methylation of phenolic products to their chemically stable methyl ether derivatives. Application of this procedure to in vitro incubations of DMBA with rat liver microsomes resulted in the isolation and identification of 4-hydroxy DMBA, 8-hydroxy DMBA and 3-hydroxy DMBA.

2534 related Products with: Identification of phenols of 7,12-dimethylbenz[a]anthracene by conversion into their methyl ethers.

rac α-Amino-3,4-dimethox 12-Amino-1-dodecanoic Aci 13-Amino-4,7,10-trioxatri Anthracene C14H10 CAS: 12 Benz[a]anthracene-7-aceti Benz[a]anthracene-7-aceti (3R)-3-[[2-(1,3-Benzodiox 4 Methylumbelliferyl alph 1 Methylnaphthalene CAS N Ofloxacin CAS Number [824 Methylene Blue Solution Methylene Blue Solution

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#380997   1979/10/26 Save this To Up

RNA polymerase from the fungus, Aspergillus nidulans. Large-scale purification of DNA-dependent RNA polymerase I (or A).

The DNA-dependent RNA polymerase I (or A) from the lower eukaryote Aspergillus nidulans has been purified on a large scale to apparent homogeneity by homogenizing the fungal hyphae in liquid nitrogen, extraction of the enzyme at high salt concentration, precipitation of RNA polymerase activity with polymin P (a polyethylene imine), elution of the RNA polymerase from the polymin P precipitate, ammonium sulphate precipitation, molecular sieving on Bio-Gel A-1.5m, binding to ion-exchangers and DNA-cellulose affinity chromatography. By this procedure 1.6 mg of RNA polymerase I can be purified over 2000-fold from 500 g wet weight of starting material with a yield of 30--35%. The isolated RNA polymerase I is stable for several months at -20 degrees C. The subunit compostion has been resolved by polyacrylamide gel electrophoresis on two-dimensional gels, using either non-denaturing of 8 M urea (pH 8.7) cylindrical gels in the first dimension and sodium dodecyl sulphate slab gels in the second dimension. The putative subunits have molecular weights of 190,000, 135,000, 63,000, 62,000, 43,000, 29,000, (28,000), 16,000 and probably 13,000 and 12,000. Two distinct forms of RNA polymerase I (Ia and Ib) have been resolved by DEAE-Sephadex A-25 chromatography showing ample differences in enzymatic properties and subunit pattern. Additional information is given on RNA polymerase II (or B) which appears to be highly insensitive to alpha-amanitin at concentrations up to 400 micrograms/ml.

2165 related Products with: RNA polymerase from the fungus, Aspergillus nidulans. Large-scale purification of DNA-dependent RNA polymerase I (or A).

Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V

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