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  • 1
    Electronic Resource
    Electronic Resource
    Trapping efficiencies of various collection solvents after supercritical fluid extraction (1993)
    Weinheim : Wiley-Blackwell
    Journal of High Resolution Chromatography 16 (1993), S. 713-716 
    Details
    ISSN: 0935-6304
    Keywords: SFE ; Supercritical carbon dioxide ; Sand ; Test mixture ; Solvent trapping ; Solvent mixtures ; Trapping efficiency ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A polarity test mix consisting of acetophenone, N, N-dimethylaniline, naphthalene, decanoic acid, 2-naphthol, and n-tetracosane was spiked onto sand, and extracted with supercritical carbon dioxide, to evaluate the collection efficiency of various solvents and solvent mixtures. Nine single collection solvent systems and four mixed collection solvent systems were studied. When one-component collection solvents were employed, quantitative (above 90%) recovery of all analytes was not possible. With mixed collection solvents, recoveries of 90% or better with all analytes studied were possible.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jhrc.1240161208
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  • 2
    Electronic Resource
    Electronic Resource
    Investigation of products arising from enzymatic digestion of advanced glycated albumin by high-performance liquid chromatography/mass spectrometry (1991)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 5 (1991), S. 624-628 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: The structural investigation of the products arising from 28 days incubation of albumin with high glucose concentration and further enzymatic hydrolysis has been carried out by means of high-performance liquid chromatography/mass spectrometry (HPLC/MS) under plasmaspray conditions. By this approach many different compounds have been detected, and for most of them, possible structures have been proposed on the basis of literature data and molecular weight assignments.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290051212
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  • 3
    Electronic Resource
    Electronic Resource
    An expanded nomenclature scheme for labeling peptide fragmentations and its use with ‘AMASS’, a computer program for generating all possible fragment ion structures from known precursors (1993)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 22 (1993), S. 31-44 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A nomenclature scheme for exhaustively labeling peptide fragment ions is proposed. The scheme is based on IUPAC nomenclature1-3 and the previously proposed Roepstorff nomenclature scheme4 used to label fragment ions in linear peptides. The descriptor used is specifically defined in order to increase the number of peptide and side chain linkages to which the nomenclature scheme can be applied compared with the Roepstorff scheme. The proposed descriptor can be used unambiguously to assign all possible fragments from linear, cyclized, branched, extended (i.e. β-amino acids) and retro inverso peptides. A significant advantage of the proposed scheme is its simple interface with the currently accepted Roepstorff scheme. This nomenclature scheme is able to label all theoretical fragments generated by the computer program ‘AMASS’. AMASS is proposed as a means of systematically calculating the mass of all possible fragment ions from known precursor structures. The program can help determine whether a peptide fragment was derived from an internal sequence fragment or a combination of side chain and backbone cleavages. The program AMASS and the proposed nomenclature scheme are used to illustrate a procedure for identifying fragment ions in the metastable product ion spectrum of somatostatin-14. We envisage that this procedure will be useful for identifying fragment ions which are characteristic of particular structural arrangements in dicyclic and polycyclic peptides.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200220105
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  • 4
    Electronic Resource
    Electronic Resource
    Capillary column gas chromatography/tandem mass spectrometry verification of chemical warfare agents (1992)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 6 (1992), S. 717-718 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: Chemical weapons use, although prohibited by the 1925 Geneva Protocol, has been reported in several armed conflicts including the Iran/Iraq war. The use of these weapons during this conflict and the concern over possible use of chemical warfare (CW) agents during the Persian Gulf war has heightened international awareness and prompted many nations to pursue with incresed vigour the signature of a new Chemical Weapons Convention. The most recent draft of the Chemical Weapons Convention contains a number of provisions aimed at developing a treaty that will enable nations to ensure compliance by all signatory nations. Compliance monitoring will be required in a number of scenarios, including the verification of alleged use, the storage and destruction of chemical weapons stocks and ensuring that industrial sites are not illegally producing CW agents. It follows from this draft treaty that compliance monitoring will require a high level of sophisticated analytical support to ensure the establishment of an enforceable treaty. The United Nations Conference on Disarmament therefore formed a multi-national Technical Group on Instrumentation to address the analytical challenges confronting signatory nations.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290061117
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  • 5
    Electronic Resource
    Electronic Resource
    Elimination of carbon monoxide by electron impact on quinoline N-oxide, carbostyril and 8-hydroxyquinolineDedicated to Professor J. D. Morrison on the occasion of his retirement from the Chair of Physical Chemistry, La Trobe University, Bundoora, Victoria, Australia. (1991)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 26 (1991), S. 247-249 
    Details
    ISSN: 0030-493X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Under electron impact, the molecular ions of quinoline N-oxide, carbostyril and 8-hydroxyquinoline lose carbon monoxide giving a fragment ion C8H7N (m/z 117), which was shown by collision-activated dissociation in each case to have the structure of the molecular ion of indole. Its formation from 8-hydroxyquinoline requires an unusual rearrangement. Isoquinoline N-oxide loses HCN rather than CO and gives a fragment which has the structure of the molecular ion of benzofuran. When the first three compounds were subjected to flash vacuum pyrolysis, quinoline N-oxide at 500-700°C gave carbostyril and indole was detected by gas chromatography/mass Spectrometry. At 900°C carbostyril and 8-hydroxyquinoline both gave indole in small amounts, detected by gas chromatography/mass Spectrometry.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/oms.1210260412
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  • 6
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    Evidence for biased gene conversion in concerted evolution of ribosomal DNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-18
    Description: Concerted evolution is the production and maintenance of homogeneity within repeated families of DNA. Two mechanisms--unequal crossing over and biased gene conversion--have been the principal explanations of concerted evolution. Concerted evolution of ribosomal DNA (rDNA) arrays is thought to be largely the result of unequal crossing over. However, concerted evolution of rDNA in parthenogenetic lizards of hybrid origin is strongly biased toward one of two parental sequences, which is consistent with biased gene conversion as the operative mechanism. The apparent gene conversions are independent of initial genome dosage and result in homogenization of rDNA arrays across all nucleolar organizer regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hillis, D M -- Moritz, C -- Porter, C A -- Baker, R J -- New York, N.Y. -- Science. 1991 Jan 18;251(4991):308-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Texas, Austin 78712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1987647" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Blotting, Southern ; DNA, Ribosomal/*genetics ; Gene Conversion ; Karyotyping ; Lizards ; Nucleic Acid Hybridization ; Parthenogenesis ; Restriction Mapping
    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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  • 7
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    Treating brain cancers (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maruyama, Y -- Fontanesi, J -- Porter, A T -- Wierzbicki, J G -- Gaspar, L -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):714-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973620" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Boron Neutron Capture Therapy ; Brain Neoplasms/*radiotherapy ; Californium/*therapeutic use ; Humans ; Neutron Capture Therapy/*methods ; Rats
    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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  • 8
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    Autoproteolysis in hedgehog protein biogenesis (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-02
    Description: Extracellular signaling proteins encoded by the hedgehog (hh) multigene family are responsible for the patterning of a variety of embryonic structures in vertebrates and invertebrates. The Drosophila hh gene has now been shown to generate two predominant protein species that are derived by an internal autoproteolytic cleavage of a larger precursor. Mutations that reduced the efficiency of autoproteolysis in vitro diminished precursor cleavage in vivo and also impaired the signaling and patterning activities of the HH protein. The two HH protein species exhibited distinctive biochemical properties and tissue distribution, and these differences suggest a mechanism that could account for the long- and short-range signaling activities of HH in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, J J -- Ekker, S C -- von Kessler, D P -- Porter, J A -- Sun, B I -- Beachy, P A -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1528-37.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985023" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Drosophila/embryology/genetics/*metabolism ; *Drosophila Proteins ; Embryo, Nonmammalian/*metabolism ; Embryonic Induction ; Gene Expression Regulation, Developmental ; Genes, Insect ; Hedgehog Proteins ; Models, Biological ; Molecular Sequence Data ; Mutation ; Protein Precursors/chemistry/genetics/metabolism ; *Protein Processing, Post-Translational ; Proteins/chemistry/genetics/*metabolism ; Serine Endopeptidases/chemistry ; *Signal Transduction
    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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  • 9
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    Dependence of calmodulin localization in the retina on the NINAC unconventional myosin (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-12
    Description: Calmodulin is a highly conserved regulatory protein found in all eukaryotic organisms which mediates a variety of calcium ion-dependent signalling pathways. In the Drosophila retina, calmodulin was concentrated in the photoreceptor cell microvillar structure, the rhabdomere, and was found in lower amounts in the sub-rhabdomeral cytoplasm. This calmodulin localization was dependent on the NINAC (neither inactivation nor afterpotential C) unconventional myosins. Mutant flies lacking the rhabdomere-specific p174 NINAC protein did not concentrate calmodulin in the rhabdomere, whereas flies lacking the sub-rhabdomeral p132 isoform had no detectable cytoplasmic calmodulin. Furthermore, a defect in vision resulted when calmodulin was not concentrated in the rhabdomeres, suggesting a role for calmodulin in the regulation of fly phototransduction. A general function of unconventional myosins may be to control the subcellular distribution of calmodulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Porter, J A -- Yu, M -- Doberstein, S K -- Pollard, T D -- Montell, C -- EY08117/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1038-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, 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/8235618" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calmodulin/*metabolism ; Drosophila ; *Drosophila Proteins ; Electroretinography ; Eye Proteins/*metabolism ; Mutation ; *Myosin Heavy Chains ; Myosins/*metabolism ; Nerve Degeneration ; Photoreceptor Cells, Invertebrate/*metabolism ; Retina/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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