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Pesquisa : D01.625.062.374 [Categoria DeCS]
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  1 / 5128 MEDLINE  
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PMID:29248767
Autor:G AG; Kamalanathan AS; Vijayalakshmi MA; Venkataraman K
Endereço:Centre for Bioseparation Technology, VIT University, Vellore- 632014, Tamil Nadu, India.
Título:Efficient purification of Apolipoprotein A1 (ApoA1) from plasma by HEA HyperCel™: An alternative approach.
Fonte:J Chromatogr B Analyt Technol Biomed Life Sci; 1073:104-109, 2018 Jan 15.
ISSN:1873-376X
País de publicação:Netherlands
Idioma:eng
Resumo:HDL-ApoA1 plays a pivotal role in the prevention of atherosclerosis and cardiovascular diseases. ApoA1 purification from blood plasma has always remained tedious, involving multiple steps, large volumes of plasma and substantial loss in the final yield of pure ApoA1. In this study, a two-step method has been developed and optimized for the purification of ApoA1 from plasma. Plasma was first subjected to 60% ammonium sulphate (NH ) SO precipitation and subsequently, ApoA1 was recovered using mixed mode chromatographic sorbent, HEA HyperCel™. ApoA1 was found to be enriched in 60% (NH ) SO supernatant that was dialyzed and injected onto HEA sorbent with 50 mM phosphate buffer pH 7.4. The bound proteins were eluted by decreasing the pH in step-gradient from pH 7.4 to pH 4.0 and subsequently to pH 3.5 using 50 mM sodium acetate buffer. Gel electrophoresis showed elution of homogeneous apoA1 at pH 3.5, with purity and yield of 63%. An interesting feature of this approach is that the purified ApoA1 was monomeric with a mass of 28,079.30 Da as confirmed by MS analysis. This simple and efficient method of purification of apoA1 serves as an alternative method which can be combined with traditional approaches and has a great potential for biochemical and clinical studies.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (APOA1 protein, human); 0 (Amines); 0 (Apolipoprotein A-I); CI4E002ZV8 (hexylamine); SU46BAM238 (Ammonium Sulfate)


  2 / 5128 MEDLINE  
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PMID:29235321
Autor:Nidialkova NA; Varbanets LD; Chernyshenko VO
Título:Isolation and purification of Bacillus thuringiensis var. israelensis IÐœV Ð’-7465 peptidase with specificity toward elastin and collagen.
Fonte:Ukr Biochem J; 88(3):18-28, 2016 May-Jun.
ISSN:2409-4943
País de publicação:Ukraine
Idioma:eng
Resumo:Peptidase of Bacillus thuringiensis var. israelensis IÐœV Ð’-7465 was isolated from culture supernatant using consecutive fractionations by an ammonium sulphate (60% saturation), ion-exchange chromatography and gel-filtration on the TSK-gels Toyoperl HW-55 and DEAE 650(M). Specific elastase (442 U∙mg of protein-1) and collagenase (212.7 U∙mg of protein-1) activities of the purified enzyme preparation were 8.0- and 6.1-fold, respectively higher than ones of the culture supernatant. Peptidase yields were 33.5% for elastase activity and 30.1% for collagenase activity. It was established that the enzyme is serine metal-dependent alkaline peptidase with Mr about 37 kDa. Maximal hydrolysis of elastin and collagen occurs at the optimum pH 8.0 and t° ­ 40 and 50 °Ð¡, respectively. The purified preparation has high stability at pH in the range of 7.0 to 10.0 and 40-50 °Ð¡.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Bacterial Proteins); 9007-34-5 (Collagen); 9007-58-3 (Elastin); EC 3.4.- (Peptide Hydrolases); SU46BAM238 (Ammonium Sulfate)


  3 / 5128 MEDLINE  
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PMID:28951283
Autor:Wälti MA; Clore GM
Endereço:Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, United States.
Título:Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.
Fonte:Protein Expr Purif; 142:8-15, 2018 Feb.
ISSN:1096-0279
País de publicação:United States
Idioma:eng
Resumo:GroEL, a prototypical member of the chaperonin class of chaperones, is a large supramocular machine that assists protein folding and plays an important role in proteostasis. GroEL comprises two heptameric rings, each of which encloses a large cavity that provides a folding chamber for protein substrates. Many questions remain regarding the mechanistic details of GroEL facilitated protein folding. Thus, data at atomic resolution of the type provided by NMR and EPR are invaluable. Such studies often require complete deuteration of GroEL, uniform or residue specific C and N isotope labeling, and the introduction of selective cysteine mutations for site-specific spin labeling. In addition, high purity GroEL is essential for detailed studies of substrate-GroEL interactions as quantitative interpretation is impossible if the cavities are already occupied and blocked by other protein substrates present in the bacterial expression system. Here we present a new purification protocol designed to provide highly pure GroEL devoid of non-specific protein substrate contamination.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Chaperonin 60); 0 (Escherichia coli Proteins); 0 (Nitrogen Isotopes); 0 (Recombinant Proteins); 8W8T17847W (Urea); SU46BAM238 (Ammonium Sulfate); Y45QSO73OB (Streptomycin)


  4 / 5128 MEDLINE  
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PMID:28818800
Autor:Johnson SA; Walsh A; Brown MR; Lute SC; Roush DJ; Burnham MS; Brorson KA
Endereço:DBRRII, Office of Biotechnology Products, Office of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, 20993, USA. Electronic address: sarah.johnson1@fda.hhs.gov.
Título:The step-wise framework to design a chromatography-based hydrophobicity assay for viral particles.
Fonte:J Chromatogr B Analyt Technol Biomed Life Sci; 1061-1062:430-437, 2017 Sep 01.
ISSN:1873-376X
País de publicação:Netherlands
Idioma:eng
Resumo:A high-salt, hydrophobic interaction chromatography (HIC) method was developed to measure the relative hydrophobicity of a diverse set of solutes. Through the careful control of buffer pH and salt concentration, this assay was then used to ascertain for the first time the relative hydrophobicity values of three different bacteriophage, four mammalian viruses, and a range of biotech medicinal proteins as benchmarked to protein standards previously characterized for hydrophobicity.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Citrates); 1Q73Q2JULR (sodium citrate); SU46BAM238 (Ammonium Sulfate)


  5 / 5128 MEDLINE  
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PMID:28622618
Autor:Yang YF; Zhang LZ; Du XP; Zhang SF; Li LJ; Jiang ZD; Wu LM; Ni H; Chen F
Endereço:College of Food and Biology Engineering, Jimei University, Xiamen, Fujian Province 361021, China; Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering Technology, Xiamen, Fujian Province 361021, China; Research Center of Food Biotechnology of Xiamen City, Xiamen, Fujian Provi
Título:Recovery and purification of limonin from pummelo [Citrus grandis] peel using water extraction, ammonium sulfate precipitation and resin adsorption.
Fonte:J Chromatogr B Analyt Technol Biomed Life Sci; 1060:150-157, 2017 Aug 15.
ISSN:1873-376X
País de publicação:Netherlands
Idioma:eng
Resumo:Limonin is a bioactive compound that is traditionally extracted from citrus seeds using organic solvents or alkaline/metal ion solutions. In the present study, pummelo [Citrus grandis] peel was investigated for limonin preparation using a novel process consisting of water extraction, ammonium sulfate precipitation and resin adsorption. The pummelo peel was determined to have 4.7mg/g limonin, which could be extracted by water and further recovered by ammonium sulfate precipitation with a yield of 2.4mg/g, which was similar to that of traditional process using ethanol extraction and vacuumed evaporation. The precipitated limonin was purified by resin adsorption and crystallization with a purity of 96.4%. In addition, the limonin was identified via the analyses of retention time, infrared spectrum and nuclear magnetic resonance. This study indicates a novel and eco-friendly process for recovering limonin, providing a new candidate for limonin preparation.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Limonins); L0F260866S (limonin); SU46BAM238 (Ammonium Sulfate)


  6 / 5128 MEDLINE  
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PMID:28423006
Autor:Kruse CPS; Basu P; Luesse DR; Wyatt SE
Endereço:Department of Environmental and Plant Biology, Ohio University, Athens, OH, United States of America.
Título:Transcriptome and proteome responses in RNAlater preserved tissue of Arabidopsis thaliana.
Fonte:PLoS One; 12(4):e0175943, 2017.
ISSN:1932-6203
País de publicação:United States
Idioma:eng
Resumo:Tissue preservation is a minimal requirement for the success of plant RNA and protein expression studies. The standard of snap-freezing in liquid nitrogen is not always practical or possible. RNAlater, a concentrated solution of ammonium and cesium sulfates, has become a standard preservative in the absence of liquid nitrogen. Here, we demonstrate the effectiveness of RNAlater in preserving both RNA and proteins in Arabidopsis thaliana tissues for use in RNAseq and LC-MS/MS analysis of proteins. While successful in preserving plant material, a transcriptomic and proteomic response is evident. Specifically, 5770 gene transcripts, 84 soluble proteins, and 120 membrane-bound proteins were found to be differentially expressed at a log-fold change of ±1 (P ≤ 0.05). This response is mirrored in the abundance of post-translational modifications, with 23 of the 108 (21.3%) phosphorylated proteins showing altered abundance at a log-fold change of ±1 (P ≤ 0.05). While RNAlater is effective in preserving biological information, our findings warrant caution in its use for transcriptomic and proteomic experiments.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Arabidopsis Proteins); 0 (Fixatives); 0 (RNA, Plant); 1KSV9V4Y4I (Cesium); 8D6R91CS62 (cesium sulfate); SU46BAM238 (Ammonium Sulfate)


  7 / 5128 MEDLINE  
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PMID:28415019
Autor:Sviben D; Forcic D; Ivancic-Jelecki J; Halassy B; Brgles M
Endereço:University of Zagreb, Centre for Research and Knowledge Transfer in Biotechnology, Rockefellerova 10, HR-10000 Zagreb, Croatia; Centre of Excellence for Viral Immunology and Vaccines, CERVirVac, Croatia.
Título:Recovery of infective virus particles in ion-exchange and hydrophobic interaction monolith chromatography is influenced by particle charge and total-to-infective particle ratio.
Fonte:J Chromatogr B Analyt Technol Biomed Life Sci; 1054:10-19, 2017 Jun 01.
ISSN:1873-376X
País de publicação:Netherlands
Idioma:eng
Resumo:Viral particles are used in medical applications as vaccines or gene therapy vectors. In order to obtain product of high purity, potency and safety for medical use purification of virus particles is a prerequisite, and chromatography is gaining increased attention to meet this aim. Here, we report on the use of ion-exchange and hydrophobic interaction chromatography on monolithic columns for purification of mumps virus (MuV) and measles virus (MeV). Efficiency of the process was monitored by quantification of infective virus particles (by 50% cell culture infective dose assay) and total virus particles, and monitoring of their size (by Nanoparticle Tracking Analysis). Ion-exchange chromatography was shown to be inefficient for MuV and best results for MeV were obtained on QA column with recovery around 17%. Purification of MuV and MeV by hydrophobic interaction chromatography resulted in recoveries around 60%. Results showed that columns with small channels (d=1.4µm) are not suitable for MuV and MeV, although their size is below 400nm, whereas columns with large channels (6µm) showed to be efficient and recoveries independent on the flow rate up to 10mL/min. Heterogeneity of the virus suspension and its interday variability mostly regarding total-to-infective particle ratio was observed. Interestingly, a trend in recovery depending on the day of the harvest was also observed for both viruses, and it correlated with the total-to-infective particle ratio, indicating influence of the virus sample composition on the chromatography results.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:SU46BAM238 (Ammonium Sulfate)


  8 / 5128 MEDLINE  
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PMID:28333451
Autor:Wu Y; Johnston MV
Endereço:Department of Chemistry and Biochemistry University of Delaware , Newark, Delaware 19716, United States.
Título:Aerosol Formation from OH Oxidation of the Volatile Cyclic Methyl Siloxane (cVMS) Decamethylcyclopentasiloxane.
Fonte:Environ Sci Technol; 51(8):4445-4451, 2017 Apr 18.
ISSN:1520-5851
País de publicação:United States
Idioma:eng
Resumo:Aerosol formation from OH oxidation of decamethylcyclopentasiloxane (D , C H O Si ), a cyclic volatile methyl siloxane (cVMS) found in consumer products, was studied in a flow-through photo-oxidation chamber with and without the presence of ammonium sulfate seed aerosol. For the unseeded experiments, chemical characterization with high-performance mass spectrometry showed that the molecular composition changed substantially with aerosol mass loading in the 1-12 µg/m range. Monomers (5 Si atoms/molecule) and dimers (10 Si atoms/molecule) dominated the mass spectra of aerosols at higher mass loadings, while ring-opened species (neither 5 nor 10 Si atoms/molecule) dominated the mass spectra of aerosols at lower mass loadings. Molecular signal intensity dependencies upon the aerosol volume/surface area ratio suggest that non-volatile ring-opened species are formed in the gas phase and assist particle formation through condensation, while dimers are formed by accretion reactions within the particle phase as the particles grow. These conclusions are supported by experiments in the presence of seed aerosol with a similar siloxane aerosol mass loading but higher volume/surface area ratio, where ring-opened species are much less prevalent than monomers or dimers and the aerosol yield is higher. Because of the importance of accretion chemistry, the aerosol yield from D oxidation is likely to be strongly dependent upon the particle size and morphology.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Aerosols); 0 (Siloxanes); SU46BAM238 (Ammonium Sulfate)


  9 / 5128 MEDLINE  
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PMID:28306524
Autor:Machado A; Lima L; Mesquita RBR; Bordalo AA
Endereço:.
Título:Improvement of the Sandell-Kolthoff reaction method (ammonium persulfate digestion) for the determination of iodine in urine samples.
Fonte:Clin Chem Lab Med; 55(9):e206-e208, 2017 Aug 28.
ISSN:1437-4331
País de publicação:Germany
Idioma:eng
Tipo de publicação: LETTER
Nome de substância:22QF6L357F (ammonium peroxydisulfate); 30K4522N6T (Cerium); 9679TC07X4 (Iodine); SU46BAM238 (Ammonium Sulfate)


  10 / 5128 MEDLINE  
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PMID:28276711
Autor:Gençer N; Yavuz E
Endereço:a Department of Chemistry , Faculty of Art and Science, Balikesir University , Balikesir , Turkey.
Título:An alternative purification method for human serum paraoxonase 1 and its interaction with methidathion.
Fonte:Arch Physiol Biochem; 123(3):159-164, 2017 Jul.
ISSN:1744-4160
País de publicação:England
Idioma:eng
Resumo:In this study, an alternative purification method for human Paraoxonase 1 (hPON1) enzyme was developed using two-step procedures, namely ammonium sulphate precipitation and Sepharose-4B-L-tyrosine-1-aminoanthracene hydrophobic interaction chromatography. SDS-polyacrylamide gel electrophoresis of the enzyme indicates a single band with an apparent MW of 43 kDa. The enzyme was purified 674-fold with a yield of 16%. Furthermore, we examined the in vitro effect of methidathion on the enzyme activity to understand the better inhibitory properties of the compound. Methidathion is a highly toxic insecticide used to control a broad spectrum of agricultural insect and mite pests. IC value was found to be 0.130 mM for the pesticide. Methidathion showed a competitive inhibition with Ki of 0.119 mM for paraoxon.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Enzyme Inhibitors); 0 (Insecticides); 0 (Organothiophosphorus Compounds); EC 3.1.8.1 (Aryldialkylphosphatase); EC 3.1.8.1 (PON1 protein, human); Q9CX8P80JW (Paraoxon); SU46BAM238 (Ammonium Sulfate); Y2P145U7KK (methidathion)



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