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  • Animals  (3)
  • spectroscopy in gels  (2)
  • GENERAL
  • Male
  • Organic Chemistry
  • ddc:330
  • 1990-1994  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Encapsulation and reactivity of the enzyme oxalate oxidase in a sol-gel derived glass (1994)
    Springer
    Journal of sol gel science and technology 2 (1994), S. 827-829 
    Details
    ISSN: 1573-4846
    Keywords: biomaterials ; sensors ; enzyme ; biosensors ; spectroscopy in gels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The enzymes oxalate oxidase and peroxidase are encapsulated in stable, optically transparent, porous silica glass matrices synthesized under mild conditions using novel sol-gel synthetic techniques. The large enzymes are immobilized, but smaller molecules such as oxalate ions pass readily through the porous glass. Upon exposure to oxalate solutions, a colored glass is formed whose absorption spectrum and changes of absorbance with time are measured. The sensitivity of the response and the time-dependence of the response are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486359
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Biomolecular materials based on sol-gel encapsulated proteins (1994)
    Springer
    Journal of sol gel science and technology 2 (1994), S. 791-795 
    Details
    ISSN: 1573-4846
    Keywords: biomaterials ; proteins ; sensor ; spectroscopy in gels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The proteins copper-zinc superoxide dismutase (CuZnSOD), cytochrome c, myoglobin, hemoglobin, and bacterio-rhodopsin are encapsulated in stable, optically transparent, porous, silica glass matrices prepared by the sol-gel method such that the biomolecules retain their characteristic reactivities and spectroscopic properties. The resulting glasses allow transport of small molecules into and out of the glasses at reasonable rates but retain the protein molecules within their pores. The transparency of the glasses enables the chemical reactions of the immobilized proteins to be monitored by means of changes in their visible absorption spectra. Silica glasses containing the immobilized proteins have similar reactivities and spectroscopic properties to those found for the proteins in solution. The enzymes glucose oxidase and peroxidase were also encapsulated in transparent silica glass matrices. Upon exposure to glucose solutions, a colored glass is formed that can be used as the active element in a solid state optically based glucose sensor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486352
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  • 3
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    Encapsulation of proteins in transparent porous silicate glasses prepared by the sol-gel method (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-28
    Description: Novel sol-gel synthetic techniques were used to immobilize copper-zinc superoxide dismutase (CuZnSOD), cytochrome c, and myoglobin (Mb) by encapsulation in stable, optically transparent, porous silica glass matrices under mild conditions such that the biomolecules retained their characteristic reactivities and spectroscopic properties. The resulting glasses allowed transport of small molecules into and out of the glasses at reasonable rates but nevertheless retained the protein molecules within their pores. Chemical reactions of the immobilized proteins could be monitored by means of changes in their visible absorption spectra. Silica glasses containing the immobilized proteins were observed to have similar reactivities and spectroscopic properties to those found for the proteins in solution. For example, encapsulated CuZnSOD was demetallated and remetallated, encapsulated ferricytochrome c was reduced and then reoxidized, and encapsulated met Mb was reduced to deoxy Mb and then reacted either with dioxygen to make oxy Mb or with carbon monoxide to make carbonyl Mb.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ellerby, L M -- Nishida, C R -- Nishida, F -- Yamanaka, S A -- Dunn, B -- Valentine, J S -- Zink, J I -- GM28222/GM/NIGMS NIH HHS/ -- T32 GM08375/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1113-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1312257" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cytochrome c Group/chemistry ; Gels ; *Glass ; Horses ; Myoglobin/chemistry ; Proteins/*chemistry ; Solutions ; Spectrum Analysis ; Superoxide Dismutase/chemistry
    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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  • 4
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    A borna virus cDNA encoding a protein recognized by antibodies in humans with behavioral diseases (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-30
    Description: Borna disease virus (BDV) causes a rare neurological disease in horses and sheep. The virus has not been classified because neither an infectious particle nor a specific nucleic acid had been identified. To identify the genome of BDV, a subtractive complementary DNA expression library was constructed with polyadenylate-selected RNA from a BDV-infected MDCK cell line. A clone (B8) was isolated that specifically hybridized to RNA isolated from BDV-infected brain tissue and BDV-infected cell lines. This clone hybridized to four BDV-specific positive strand RNAs (10.5, 3.6, 2.1, and 0.85 kilobases) and one negative strand RNA (10.5 kilobases) in BDV-infected rat brain. Nucleotide sequence analysis of the clone suggested that it represented a full-length messenger RNA which contained several open reading frames. In vitro transcription and translation of the clone resulted in the synthesis of the 14- and 24-kilodalton BDV-specific proteins. The 24-kilodalton protein, when translated in vitro from the clone, was recognized by antibodies in the sera of patients (three of seven) with behavioral disorders. This BDV-specific clone will provide the means to isolate the other BDV-specific nucleic acids and to identify the virus responsible for Borna disease. In addition, the significance of BDV or a BDV-related virus as a human pathogen can now be more directly examined.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉VandeWoude, S -- Richt, J A -- Zink, M C -- Rott, R -- Narayan, O -- Clements, J E -- RR00130/RR/NCRR NIH HHS/ -- RR07002/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 30;250(4985):1278-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Colorado State University, Lab Animal Resources, Fort Collins 80532.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2244211" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Viral/*blood ; Borna Disease/*microbiology ; Borna disease virus/*genetics/immunology ; Brain/microbiology ; Cloning, Molecular ; DNA/*genetics ; Fluorescent Antibody Technique ; Humans ; Immunoblotting ; Mental Disorders/*microbiology ; Molecular Sequence Data ; Molecular Weight ; Nucleic Acid Hybridization ; RNA, Messenger/analysis/genetics ; RNA, Viral/analysis/genetics ; Rats ; Transcription, Genetic ; Viral Proteins/*genetics/immunology
    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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  • 5
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    Expression directed from HIV long terminal repeats in the central nervous system of transgenic mice (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-11
    Description: Infection with the human immunodeficiency virus (HIV) is frequently accompanied by the AIDS (acquired immunodeficiency syndrome) dementia complex. The role of specific HIV genetic elements in the pathogenesis of central nervous system (CNS) disease is not clear. Transgenic mice were constructed that contained the long terminal repeats (LTRs) of two CNS-derived strains and a T cell tropic strain of HIV-1. Only mice generated with CNS-derived LTRs directed expression in the CNS, particularly in neurons. Thus, some strains of HIV-1 have a selective advantage for gene expression in the brain, and neurons can supply the cellular factors necessary for their transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corboy, J R -- Buzy, J M -- Zink, M C -- Clements, J E -- AI27297/AI/NIAID NIH HHS/ -- AI28748/AI/NIAID NIH HHS/ -- NS07000/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1804-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Comparative Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1465618" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*physiology ; Central Nervous System/*physiology ; Female ; Gene Expression ; *HIV Long Terminal Repeat ; HIV-1/*genetics ; Intestine, Small/physiology ; Lung/physiology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Inbred DBA ; Mice, Transgenic ; Ocular Physiological Phenomena ; Organ Specificity ; RNA, Messenger/analysis/*metabolism ; Recombinant Fusion Proteins/metabolism ; Spinal Cord/physiology ; Thymus Gland/physiology ; beta-Galactosidase/genetics/metabolism
    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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