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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 45 (1995), S. 27-32 
    ISSN: 0006-3592
    Keywords: esterification ; lipase ; glycerides ; organic solvent ; surfactant ; bioconversion ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Several surfactant-coated enzymes have been prepared by coating lipases of various origins with a nonionic surfactant, glutamic acid dioleylester ribitol (2C18Δ9GE). Enzymatic interesterification of tripalmitin with oleic acid using the surfactant-coated lipase was carried out in organic media. The surfactant-coated lipases could effectively catalyze the interesterification of glycerides better than did the powder lipases. A suitable organic solvent was an aliphatic hydrocarbon such as isooctane. The enzymatic activity for the interesterification strongly depended on the origin of the lipase. The surfactant-coated lipase prepared by Mucor javanicus showed the highest enzymatic activity for the interesterification of glycerides, although its powder lipase did not show enzymatic activity. Selective interesterification of glycerides could be performed by adjusting the concentration ratio of oleic acid to tripalmitin in isooctane. Di-substituted glyceride could be selectively produced when the concentration ratio of carboxylic acid to glycerides was 7. © 1995 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 57 (1998), S. 620-623 
    ISSN: 0006-3592
    Keywords: protein refolding ; reversed micelles ; solid-liquid extraction ; RNase A ; DNA ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This article reports that a reversed micellar solution is useful for refolding proteins directly from a solid source. The solubilization of denatured RNase A, which had been prepared by reprecipitation from the denaturant protein solution, into reversed micelles formulated with sodium di-2-ethylhexyl sulfosuccinate (AOT) has been investigated by a solid-liquid extraction system. This method is an alternative to the ordinary protein extraction in reversed micelles based on the liquid-liquid extraction. The solid-liquid extraction method was found to facilitate the solubilization of denatured proteins more efficiently in the reversed micellar media than the ordinary phase transfer method of liquid extraction. The refolding of denatured RNase A entrapped in reversed micelles was attained by adding a redox reagent (reduced and oxidized glutathion). Enzymatic activity of RNase A was gradually recovered with time in the reversed micelles. The denatured RNase A was completely refolded within 30 h. In addition, the efficiency of protein refolding was enhanced when reversed micelles were applied to denatured RNase A containing a higher protein concentration that, in the case of aqueous media, would lead to protein aggregation. The solid-liquid extraction technique using reversed micelles affords better scale-up advantages in the direct refolding process of insoluble protein aggregates. ©1998 John Wiley & Sons, Inc. Biotechnol Bioeng 57: 620-623, 1998.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 54 (1997), S. 26-32 
    ISSN: 0006-3592
    Keywords: reversed micelle ; microemulsion ; protein extraction ; surfactant ; bioseparation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: New surfactants have been synthesized for potential use in reversed micellar protein extraction operations. Preferential solubility of the surfactant in an aliphatic solvent such as hexane, heptane, or isooctane and the formation of reversed micelles accompanied with solubilization of significant quantities of water can be achieved by using strongly hydrophobic, twin alkyl chains as the hydrophobic moiety. Different surfactants having identical water-solubilizing capacities can have significantly different behavior in protein extractions, where extraction efficiency appears to be governed by the nature of the interfacial complex that forms between surfactants and proteins. Bulky surfactant chains provide a steric hindrance to the adsorption of the surfactant to the protein surface, thus inhibiting solvation of the protein/surfactant complex, and hence protein extraction. Under these conditions, a precipitate forms either in the bulk aqueous phase or at the interface. Surfactants that can form a close-packed complex with the protein are excellent protein-solubilizing agents. Dioleyl phosphoric acid (DOLPA) appears to be the best surfactant currently available for protein extraction. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 54: 26-32, 1997.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 55 (1997), S. 455-460 
    ISSN: 0006-3592
    Keywords: enzyme ; biocatalyst ; lipase ; organic solvent ; emulsion ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A novel preparation method for surfactant-lipase complexes has been developed utilizing water in oil emulsions. In order to optimize the preparation conditions, we have investigated the effects of several operational parameters on the enzymatic activity of the surfactant-lipase complexes in organic media. When a nonionic surfactant was employed under optimal preparation conditions [alkaline pH 8-10, organic/aqueous = 90/10 (v/v), concentration of surfactant, 10 mM[, the surfactant-lipase complex efficiently catalyzed the esterification of benzyl alcohol with lauric acid in organic media. The esterification rate of the surfactant-lipase complex was increased over 16-fold relative to the native powder lipase. Furthermore, the lipase complex showed high storage stability. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 55: 455-460, 1997.
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  • 5
    ISSN: 0173-0835
    Keywords: Amphotericin B ; Fungizone ; Membrane filter ; Micellar electrokinetic capillary chromatography ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The determination of amphotericin B, an antifungal agent, was developed using micellar electrokinetic capillary chromatography (MEKC) with a diode array detector. Repeatability and intermediate precision of MEKC analysis were acceptable. A high correlation was found between amphotericin B levels in pharmaceutical solutions obtained by MEKC and those by high-performance liquid chromatography (HPLC) (r = 0.994). This MEKC method is therefore useful for the determination of amphotericin B. The concentration of amphotericin B did not significantly change after filtration through polyethersulfone (PES, 0.2 μm) and polyvinylidene difluoride (PVDF, 0.45 μm) membrane filters. When the Fungizone injection was filtered through PES (0.2 μm) and added to 5% dextrose for injection (500 mL), particulate matters larger than 10 μm decreased by 64% to a level under the standard defined by United States Pharmacopoeia (USP XXIII). PVDF filtration (0.45 μm) did not have this effect. Our results suggest that filtration of Fungizone injection through PES (0.2 μm) membrane filters is recommended for the preparation of intravenous amphotericin B fluid.
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  • 6
    ISSN: 0884-3996
    Keywords: Singlet oxygen ; Cypridina luciferin analogue ; MCLA ; quenching of singlet oxygen ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The rate constants for [1O2] [MCLA] and [1O2][NaN3] were measured by quenching the near-infrared emission (1Δg→3∑g) in steady state with MCLA and NaN3, respectively. 1O2 was constantly generated by energy transfer to O2 from Ar laser-excited Rose Bengal. The Stern - Volmer plots yielded the second-order rate constants of 2.94 × 109 M-1 S-1 and 3.83 × 108 M-1 S-1 for quenching 1O2 with MCLA and NaN3 in water at pH 5.4, respectively. The 1O2 + MCLA reaction emitted light with maximum at 465 nm at pD 4.5 identical to the O2- + MCLA reaction.
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  • 7
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 1 (1987), S. 181-188 
    ISSN: 0884-3996
    Keywords: Lampteromyces ; bioluminescence ; riboflavin ; light emitter ; mushroom ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The bioluminescence of the luminous mushroom, Lampteromyces japonicus, was studied by using the mushroom gills and also the luminous mycelia, the latter being cultured from the isolated spores and grown in a potato sucrose medium. The luminescence intensity of the mushroom gills and the cultured mycelia was measured in an aqueous suspension under various conditions. The original intensity was enhanced by exposing the luminous cells to oxygen for several hours or to acids or bases for a short period. This enhancement enabled measurement of their bioluminescence spectra which were identical to the fluorescence spectrum of riboflavin, having a maximum at 524 nm. The green fluorescent substance was extracted with cold water from the mushroom and it was identified as riboflavin by spectroscopic and chromatographic analyses. Riboflavin was concluded to be the light emitter of this mushroom.
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  • 8
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 2 (1988), S. 73-79 
    ISSN: 0884-3996
    Keywords: bioluminescence ; fluorescence ; Dyakia striata ; snail ; mollusc ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The luminescent land snail Dyakia striata displayed a bioluminescence spectrum with a maximum wavelength of 515 nm. A green fluorescent substance extracted from the photogenic organ of an adult snail had a similar wavelength maximum but its fluorescence spectrum differed from that of flavin chromophore substances involved in light emission in some other luminescent organisms.
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  • 9
    Publication Date: 2001-05-08
    Description: Glial cells express a variety of neurotransmitter receptors. Notably, Bergmann glial cells in the cerebellum have Ca2+-permeable alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPARs) assembled without the GluR2 subunit. To elucidate the role of these Ca2+-permeable AMPARs, we converted them into Ca2+-impermeable receptors by adenoviral-mediated delivery of the GluR2 gene. This conversion retracted the glial processes ensheathing synapses on Purkinje cell dendritic spines and retarded the removal of synaptically released glutamate. Furthermore, it caused multiple innervation of Purkinje cells by the climbing fibers. Thus, the glial Ca2+-permeable AMPARs are indispensable for proper structural and functional relations between Bergmann glia and glutamatergic synapses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iino, M -- Goto, K -- Kakegawa, W -- Okado, H -- Sudo, M -- Ishiuchi, S -- Miwa, A -- Takayasu, Y -- Saito, I -- Tsuzuki, K -- Ozawa, S -- New York, N.Y. -- Science. 2001 May 4;292(5518):926-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gunma University School of Medicine, Maebashi, Gunma 371-8511, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11340205" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Animals ; Astrocytes/cytology/*physiology ; Calcium/*metabolism ; Calcium Signaling ; Excitatory Postsynaptic Potentials ; Genetic Vectors ; Green Fluorescent Proteins ; In Vitro Techniques ; Luminescent Proteins/genetics ; Membrane Potentials ; Patch-Clamp Techniques ; Permeability ; Purkinje Cells/cytology/*physiology ; Rats ; Receptors, AMPA/genetics/*metabolism ; Synapses/metabolism/*physiology ; *Synaptic Transmission ; Transfection ; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2009-08-13
    Description: Influenza A viruses cause recurrent outbreaks at local or global scale with potentially severe consequences for human health and the global economy. Recently, a new strain of influenza A virus was detected that causes disease in and transmits among humans, probably owing to little or no pre-existing immunity to the new strain. On 11 June 2009 the World Health Organization declared that the infections caused by the new strain had reached pandemic proportion. Characterized as an influenza A virus of the H1N1 subtype, the genomic segments of the new strain were most closely related to swine viruses. Most human infections with swine-origin H1N1 influenza viruses (S-OIVs) seem to be mild; however, a substantial number of hospitalized individuals do not have underlying health issues, attesting to the pathogenic potential of S-OIVs. To achieve a better assessment of the risk posed by the new virus, we characterized one of the first US S-OIV isolates, A/California/04/09 (H1N1; hereafter referred to as CA04), as well as several other S-OIV isolates, in vitro and in vivo. In mice and ferrets, CA04 and other S-OIV isolates tested replicate more efficiently than a currently circulating human H1N1 virus. In addition, CA04 replicates efficiently in non-human primates, causes more severe pathological lesions in the lungs of infected mice, ferrets and non-human primates than a currently circulating human H1N1 virus, and transmits among ferrets. In specific-pathogen-free miniature pigs, CA04 replicates without clinical symptoms. The assessment of human sera from different age groups suggests that infection with human H1N1 viruses antigenically closely related to viruses circulating in 1918 confers neutralizing antibody activity to CA04. Finally, we show that CA04 is sensitive to approved and experimental antiviral drugs, suggesting that these compounds could function as a first line of defence against the recently declared S-OIV pandemic.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2748827/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2748827/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Itoh, Yasushi -- Shinya, Kyoko -- Kiso, Maki -- Watanabe, Tokiko -- Sakoda, Yoshihiro -- Hatta, Masato -- Muramoto, Yukiko -- Tamura, Daisuke -- Sakai-Tagawa, Yuko -- Noda, Takeshi -- Sakabe, Saori -- Imai, Masaki -- Hatta, Yasuko -- Watanabe, Shinji -- Li, Chengjun -- Yamada, Shinya -- Fujii, Ken -- Murakami, Shin -- Imai, Hirotaka -- Kakugawa, Satoshi -- Ito, Mutsumi -- Takano, Ryo -- Iwatsuki-Horimoto, Kiyoko -- Shimojima, Masayuki -- Horimoto, Taisuke -- Goto, Hideo -- Takahashi, Kei -- Makino, Akiko -- Ishigaki, Hirohito -- Nakayama, Misako -- Okamatsu, Masatoshi -- Takahashi, Kazuo -- Warshauer, David -- Shult, Peter A -- Saito, Reiko -- Suzuki, Hiroshi -- Furuta, Yousuke -- Yamashita, Makoto -- Mitamura, Keiko -- Nakano, Kunio -- Nakamura, Morio -- Brockman-Schneider, Rebecca -- Mitamura, Hiroshi -- Yamazaki, Masahiko -- Sugaya, Norio -- Suresh, M -- Ozawa, Makoto -- Neumann, Gabriele -- Gern, James -- Kida, Hiroshi -- Ogasawara, Kazumasa -- Kawaoka, Yoshihiro -- HHNSN266200700010C/NS/NINDS NIH HHS/ -- HHSN266200700010C/PHS HHS/ -- HHSN272200800060C/AI/NIAID NIH HHS/ -- R01 AI069274/AI/NIAID NIH HHS/ -- R01 AI069274-04/AI/NIAID NIH HHS/ -- U19 AI070503/AI/NIAID NIH HHS/ -- England -- Nature. 2009 Aug 20;460(7258):1021-5. doi: 10.1038/nature08260.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Shiga University of Medical Science, Ohtsu, Shiga 520-2192, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19672242" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Viral/immunology ; Antiviral Agents/pharmacology ; Cell Line ; Dogs ; Female ; Ferrets/virology ; HN Protein/metabolism ; Humans ; Influenza A Virus, H1N1 Subtype/drug effects/enzymology/pathogenicity/*physiology ; Lung/immunology/pathology/virology ; Macaca fascicularis/immunology/virology ; Male ; Mice ; Mice, Inbred BALB C ; Neutralization Tests ; Orthomyxoviridae Infections/immunology/transmission/virology ; Primate Diseases/pathology/virology ; Swine/*virology ; Swine Diseases/pathology/virology ; Swine, Miniature/virology ; Virus Replication
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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