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  • 1
    Electronic Resource
    Electronic Resource
    Wheat β-amylase behaviour regarding salt promoted adsorption processes (1998)
    Springer
    Chromatographia 48 (1998), S. 209-214 
    Details
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; Covalent chromatography ; Thiophilic and hydrophobic ligands ; Wheat β-amylase ; Salt promoted adsorption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The behaviour of wheat β-amylase from crude extracts in chromatography on agarose gels substituted with different ligand types was investigated. The enzyme displayed high salt promoted adsorption onto thiophilic gels provided with sulfone-thioether and 2-thiopyridine ligands. Quantitative recovery of the enzyme was easily accomplished by elution with buffer in the absence of Na2SO4. The 3-(2-pyridylthio)-2-hydroxypropylagarose (PyS-gel) also allowed elimination of pigments present in the wheat extract. These pigments showed no adsorption onto the gel, thus regeneration is easily achieved, allowing its re-use. The enzyme also displayed strong salt-dependent adsorption onto adsorbents provided with pyridyldisulfide moieties, but in this case enzyme binding was due to its thiol content since elution was achieved mainly through reduction with DTT. When the enzyme was chromatographed on a series of hydrophobic alkyl ligands in the presence of 0.5 M sodium sulphate, it was partially adsorbed on pentylagarose and quantitatively adsorbed on hexyl-agarose, elution being easily performed by sodium sulphate-free buffer. This behaviour was markedly different from that towards phenyl-Sepharose, to which the enzyme was strongly adsorbed and which required much more drastic elution conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02467673
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Salt promoted adsorption chromatography of malted barley amylases (1994)
    Springer
    Chromatographia 38 (1994), S. 232-234 
    Details
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; Thiophilic interaction chromatography ; Hydrophobic interaction chromatography ; Salt-promoted adsorption ; Malted barley amylases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A sequence for the fractionation of the amylasic components from a malted barley extract is proposed using two salt-promoted, adsorption processes: thiophilic interaction chromatography (TIC) and hydrophobic interaction chromatography (HIC). Two fractions containing α-amylase activity were recovered during the thiophilic chromatography; the first was resolved in to α-amylase I and β-amylase I by HIC on a phenyl-sepharose column; an enrichment factor of 32 was achieved for α-amylase I. The other amylasic component eluted from the thiophilic gel was characterized as α-amylase II. Although the adsorption of malt amylases on phenylsepharose and the thiophilic adsorbent is salt promoted, the interactions involved in each case are clearly distinguished by the different behaviour and disparate salt effects.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02290342
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  • 3
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    Campaign tactics and grants don't mix (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-05-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maojo, Victor -- Pazos, Juan -- Kulikowski, Casimir A -- England -- Nature. 2013 May 23;497(7450):439. doi: 10.1038/497439b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23698436" target="_blank"〉PubMed〈/a〉
    Keywords: Europe ; Financing, Organized/economics/*organization & administration ; Neurosciences/trends ; Peer Review, Research/standards ; *Politics ; *Public Policy ; Social Media/utilization ; United States
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    Reactome array: forging a link between metabolome and genome (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-10
    Description: We describe a sensitive metabolite array for genome sequence-independent functional analysis of metabolic phenotypes and networks, the reactomes, of cell populations and communities. The array includes 1676 dye-linked substrate compounds collectively representing central metabolic pathways of all forms of life. Application of cell extracts to the array leads to specific binding of enzymes to cognate substrates, transformation to products, and concomitant activation of the dye signals. Proof of principle was shown by reconstruction of the metabolic maps of model bacteria. Utility of the array for unsequenced organisms was demonstrated by reconstruction of the global metabolisms of three microbial communities derived from acidic volcanic pool, deep-sea brine lake, and hydrocarbon-polluted seawater. Enzymes of interest are captured on nanoparticles coated with cognate metabolites, sequenced, and their functions unequivocally established.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beloqui, Ana -- Guazzaroni, Maria-Eugenia -- Pazos, Florencio -- Vieites, Jose M -- Godoy, Marta -- Golyshina, Olga V -- Chernikova, Tatyana N -- Waliczek, Agnes -- Silva-Rocha, Rafael -- Al-Ramahi, Yamal -- La Cono, Violetta -- Mendez, Carmen -- Salas, Jose A -- Solano, Roberto -- Yakimov, Michail M -- Timmis, Kenneth N -- Golyshin, Peter N -- Ferrer, Manuel -- New York, N.Y. -- Science. 2009 Oct 9;326(5950):252-7. doi: 10.1126/science.1174094.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CSIC, Institute of Catalysis, 28049 Madrid, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19815770" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/genetics/metabolism ; Bacteria/genetics/*metabolism ; Bacterial Proteins/metabolism ; Computational Biology ; Ecosystem ; Enzymes/*metabolism ; Enzymes, Immobilized ; Genome, Archaeal ; *Genome, Bacterial ; Hot Springs/microbiology ; *Metabolic Networks and Pathways ; *Metabolome ; Metabolomics/*methods ; Microarray Analysis/*methods ; Nanoparticles ; Pseudomonas putida/genetics/metabolism ; Seawater/microbiology ; Streptomyces coelicolor/genetics/metabolism ; Water Microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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