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  • 1
    Publication Date: 1990-04-27
    Description: Affinity-purified, polyclonal antibodies to the gamma subunit of the dihydropyridine (DHP)-sensitive, voltage-dependent calcium channel have been used to isolate complementary DNAs to the rabbit skeletal muscle protein from an expression library. The deduced primary structure indicates that the gamma subunit is a 25,058-dalton protein that contains four transmembrane domains and two N-linked glycosylation sites, consistent with biochemical analyses showing that the gamma subunit is a glycosylated hydrophobic protein. Nucleic acid hybridization studies indicate that there is a 1200-nucleotide transcript in skeletal muscle but not in brain or heart. The gamma subunit may play a role in assembly, modulation, or the structure of the skeletal muscle calcium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jay, S D -- Ellis, S B -- McCue, A F -- Williams, M E -- Vedvick, T S -- Harpold, M M -- Campbell, K P -- HL-14388/HL/NHLBI NIH HHS/ -- HL-37187/HL/NHLBI NIH HHS/ -- HL-39265/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 27;248(4954):490-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City 52242.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2158672" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Calcium Channels/drug effects/physiology ; DNA/isolation & purification ; Dihydropyridines/*pharmacology ; Disulfides ; Electrophoresis, Polyacrylamide Gel ; Immunoassay ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Muscles/*analysis ; Nucleic Acid Hybridization ; Protein Conformation ; RNA, Messenger/analysis ; Rabbits ; Sequence Homology, Nucleic Acid
    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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  • 2
    Publication Date: 1993-07-23
    Description: Calcium channels play an important role in regulating various neuronal processes, including synaptic transmission and cellular plasticity. The N-type calcium channels, which are sensitive to omega-conotoxin, are involved in the control of transmitter release from neurons. A functional N-type calcium channel complex was purified from rabbit brain. The channel consists of a 230-kilodalton subunit (alpha 1B) that is tightly associated with a 160-kilodalton subunit (alpha 2 delta), a 57-kilodalton subunit (beta 3), and a 95-kilodalton glycoprotein subunit. The complex formed a functional calcium channel with the same pharmacological properties and conductance as those of the native omega-conotoxin-sensitive calcium channel in neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Witcher, D R -- De Waard, M -- Sakamoto, J -- Franzini-Armstrong, C -- Pragnell, M -- Kahl, S D -- Campbell, K P -- New York, N.Y. -- Science. 1993 Jul 23;261(5120):486-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City 52242.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8392754" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Chemistry/*physiology ; Calcium Channel Blockers/metabolism ; Calcium Channels/chemistry/*physiology ; Immunochemistry ; Peptide Fragments/physiology ; Peptides/metabolism ; Rabbits ; Radioligand Assay ; Receptors, Neurotransmitter/chemistry/isolation & purification/*physiology ; omega-Conotoxin GVIA
    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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  • 3
    Publication Date: 1988-09-23
    Description: Complementary DNAs were isolated and used to deduce the primary structures of the alpha 1 and alpha 2 subunits of the dihydropyridine-sensitive, voltage-dependent calcium channel from rabbit skeletal muscle. The alpha 1 subunit, which contains putative binding sites for calcium antagonists, is a hydrophobic protein with a sequence that is consistent with multiple transmembrane domains and shows structural and sequence homology with other voltage-dependent ion channels. In contrast, the alpha 2 subunit is a hydrophilic protein without homology to other known protein sequences. Nucleic acid hybridization studies suggest that the alpha 1 and alpha 2 subunit mRNAs are expressed differentially in a tissue-specific manner and that there is a family of genes encoding additional calcium channel subtypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ellis, S B -- Williams, M E -- Ways, N R -- Brenner, R -- Sharp, A H -- Leung, A T -- Campbell, K P -- McKenna, E -- Koch, W J -- Hui, A -- New York, N.Y. -- Science. 1988 Sep 23;241(4873):1661-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute Biotechnology/Industrial Associates, Inc., La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2458626" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcium/*metabolism ; Calcium Channel Blockers/pharmacology ; Cloning, Molecular ; *Dna ; DNA Restriction Enzymes ; Dihydropyridines/pharmacology ; *Ion Channels/drug effects ; Molecular Sequence Data ; Organ Specificity ; *Peptide Mapping ; RNA, Messenger/biosynthesis ; Rabbits ; Sequence Homology, Nucleic Acid
    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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  • 4
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 22 (1976), S. 828-832 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The sorption and rate of permeation of scopolamine base in human skin have been measured as a function of drug concentration in aqueous solution contacting the stratum corneum surface of the skin. The sorption isotherm is nonlinear, and the apparent penetrant diffusivity computed from steady state permeation data is greater than that estimated from unsteady state (time lag) measurements.By assuming that sorption occurs by both ordinary dissolution and binding of penetrant to immobile sites in the membrane, the experimental sorption isotherm can be predicted, and the disparity between steady state and time lag diffusivities can be reconciled.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 23 (1977), S. 810-816 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effect of the presence of dimethyl sulfoxide (in admixture with water) on the sorption and permeation rate of scopolamine base in human skin in vitro has been measured as a function of drug concentration in aqueous solution. The equilibrium sorption of scopolamine by skin from solution appears to be unaffected by the presence of even high concentrations of dimethyl sulfoxide in the solution phase. In the absence of a transdermal gradient of DMSO (or water), the permeability of skin to scopolamine in the presence of DMSO is about twofold higher than in its absence, suggesting that the diffusivity of scopolamine in the stratum corneum is somewhat elevated by the solvating action of DMSO.When, however, a gradient of DMSO concentration is impressed across the skin (irrespective of whether that gradient is of the same or opposite sign to that of the drug), the permeability of the skin to scopolamine is increased by one to two orders of magnitude. Microscopic examination of the skin subjected to such treatment reveals marked swelling, distortion, and intercellular delamination of the stratum corneum, which is only partially reversible following complete extraction with water. These effects are believed due to development of very high osmotic stresses produced within the stratum corneum, as both water and DMSO are transported into the tissue.
    Additional Material: 6 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    Stamford, Conn. [u.a.] : Wiley-Blackwell
    Polymer Engineering and Science 20 (1980), S. 36-39 
    ISSN: 0032-3888
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: The dual sorption theory has been extended to the transport of drug molecules through human skin in vitro. By assuming that sorption of drug molecules occurs by both dissolution and binding of drug to immobile sites in the skin, the experimental sorption isotherm can be predicted, and the disparity between steady state and time lag diffusivities can be reconciled. Furthermore, the dual sorption model has been used to develop techniques for controlling these sorption transport processes in order to rapidly achieve predictable transdermal drug delivery in vivo.
    Additional Material: 6 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 29 (1995), S. 127-131 
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: A method of tissue digestion using sodium hydroxide was applied to the isolation and recovery of ultra-high-molecular-weight polyethylene (UHMWPE) particles from tissues around failed total hip replacements. Density gradient ultracentrifugation of the digested tissues was performed to separate the UHMWPE from cell debris and other particulates. Fourier transform infrared spectroscopy and differential scanning calorimetry (DSC) verified that the recovered particles were UHMWPE. When viewed by scaning electron microscopy, individual particles were clearly observed and were either rounded or elongated. The majority were submicron in size. The application of this method to the study or particles from periprosthetic tissues may elucidate aspects of biomaterial particles size and shape that are important to the biologic response to, and clinical outcome of, total joint replacement. © 1995 John wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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