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  • Chromatography
  • American Association for the Advancement of Science (AAAS)  (7)
  • American Chemical Society  (1)
  • Springer Science + Business Media
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  • 1
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    Production of two highly abundant 2-methyl-branched fatty acids by blooms of the globally significant marine cyanobacteria Trichodesmium erythraeum (2021)
    American Chemical Society
    Details
    Publication Date: 2022-05-27
    Description: © The Author(s), 2021. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Gosselin, K. M., Nelson, R. K., Spivak, A. C., Sylva, S. P., Van Mooy, B. A. S., Aeppli, C., Sharpless, C. M., O’Neil, G. W., Arrington, E. C., Reddy, C. M., & Valentine, D. L. Production of two highly abundant 2-methyl-branched fatty acids by blooms of the globally significant marine cyanobacteria Trichodesmium erythraeum. ACS Omega, 6(35), (2021): 22803–22810, https://doi.org/10.1021/acsomega.1c03196.
    Description: The bloom-forming cyanobacteria Trichodesmium contribute up to 30% to the total fixed nitrogen in the global oceans and thereby drive substantial productivity. On an expedition in the Gulf of Mexico, we observed and sampled surface slicks, some of which included dense blooms of Trichodesmium erythraeum. These bloom samples contained abundant and atypical free fatty acids, identified here as 2-methyldecanoic acid and 2-methyldodecanoic acid. The high abundance and unusual branching pattern of these compounds suggest that they may play a specific role in this globally important organism.
    Description: This work was funded with grants from the National Science Foundation grants OCE-1333148, OCE-1333162, and OCE-1756254 and the Woods Hole Oceanographic Institution (IR&D). GCxGC analysis made possible by WHOI’s Investment in Science Fund.
    Keywords: Lipids ; Alkyls ; Bacteria ; Genetics ; Chromatography
    Repository Name: Woods Hole Open Access Server
    Type: Article
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  • 2
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    Long-range electrostatic trapping of single-protein molecules at a liquid-solid interface (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-11
    Description: The motion of single, dye-labeled protein molecules was monitored at various pH and ionic strengths within the 180-nanometer-thick evanescent-field layer at a fused-silica surface. Below the isoelectric point, molecules partitioning into the excitation region increased in number but maintained a random spatial distribution, implying that surface charge can influence the charged protein at distances beyond that of the electrical double-layer thickness. The residence times of the molecules in the interfacial layer also increased below the isoelectric point. However, immobilization on the solid surface for extended periods was not observed. Histograms of residence times exhibit nearly identical asymmetry as the corresponding elution peaks in capillary electrophoresis. These results are a direct verification of the statistical theory of chromatography at the single-molecule level, with the caveat that long-range trapping rather than adsorption is the dominant mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, X H -- Yeung, E S -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1650-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ames Laboratory-U.S. Department of Energy and Department of Chemistry, Iowa State University, Ames, IA 50011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9733506" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Chromatography ; Concanavalin A/*chemistry ; Diffusion ; Electrophoresis, Capillary ; Fluorescence ; Hydrogen-Ion Concentration ; Isoelectric Point ; Osmolar Concentration ; Physicochemical Phenomena ; Proteins/*chemistry ; Rhodamines ; Static Electricity
    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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  • 3
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    Fluorous mixture synthesis: a fluorous-tagging strategy for the synthesis and separation of mixtures of organic compounds (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-07
    Description: The solution-phase synthesis of organic compounds as mixtures rather than in individual pure form offers efficiency advantages that are negated by the difficulty in separating and identifying the components of the final mixture. Here, a strategy for mixture synthesis that addresses these separation and identification problems is presented. A series of organic substrates was tagged with a series of fluorous tags of increasing fluorine content. The compounds were then mixed, and multistep reactions were conducted to make enantiomers or analogs of the natural product mappicine. The resulting tagged products were then demixed by fluorous chromatography (eluting in order of increasing fluorine content) to provide the individual pure components of the mixture, which were detagged to release the final products.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Luo, Z -- Zhang, Q -- Oderaotoshi, Y -- Curran, D P -- New York, N.Y. -- Science. 2001 Mar 2;291(5509):1766-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Center for Combinatorial Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11230688" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaloids/*chemical synthesis/chemistry ; Chromatography ; Chromatography, Gel/*methods ; Combinatorial Chemistry Techniques ; *Fluorine/analysis ; Organic Chemicals/*chemical synthesis/isolation & purification ; Spectrum Analysis ; Stereoisomerism
    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
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    Production of mammastatin, a tissue-specific growth inhibitor, by normal human mammary cells (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-06-30
    Description: The growth of human mammary cells may be regulated by a balance between growth stimulatory and growth inhibitory pathways. Polypeptides of 47 and 65 kilodaltons (mammastatin) were isolated from conditioned medium of normal human mammary cells. Monoclonal antibodies against mammastatin were generated that blocked its activity and were used for purification and further characterization of the protein. Mammastatin inhibited the growth of 5 transformed human mammary cell lines, but had no effect on the growth of 11 transformed human cell lines derived from nonmammary tissues. Mammastatin appeared to be a heat-labile protein distinct from transforming growth factor-beta (TGF-beta). By immunoperoxidase staining it was detected in cultured normal human mammary cells, but was decreased in transformed mammary cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ervin, P R Jr -- Kaminski, M S -- Cody, R L -- Wicha, M S -- New York, N.Y. -- Science. 1989 Jun 30;244(4912):1585-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Michigan Cancer Center, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2662405" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Breast/analysis/cytology/*metabolism ; Breast Neoplasms/metabolism/pathology ; Cell Division ; Cell Line, Transformed ; Chromatography ; Chromatography, Gel ; Electrophoresis, Polyacrylamide Gel ; Epithelium/metabolism ; Female ; Growth Inhibitors/*biosynthesis/isolation & purification/pharmacology ; Hot Temperature ; Humans ; Immunoassay ; Immunoenzyme Techniques ; Molecular Weight ; *Peptide Biosynthesis ; Peptides/isolation & purification/pharmacology ; Trypsin/pharmacology ; Tumor Cells, Cultured
    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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  • 5
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    Self-assembling dendrimers (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-23
    Description: Hydrogen bond-mediated self-assembly is a powerful strategy for generating large structures from smaller subunits. The synthesis of molecules containing two isophthalic acid units covalently attached to a rigid aromatic spacer is described. By normal pairing of carboxylic acids into hydrogen-bonded dimers, these molecules self-assemble in organic solvents to form either a series of linear aggregates or a cyclic hexamer. These molecules were linked to the core of a family of polyether dendrimers, which caused the hexamer to be formed preferentially. The stability of the hexamer depended on the generation number of the dendrimer. The largest of these hydrogen-bonded macromolecular assemblies is roughly disk-shaped with a 9-nanometer diameter and a 2-nanometer thickness. Its size and molecular mass (34,000 daltons) are comparable to that of small proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zimmerman, S C -- Zeng, F -- Reichert, D E -- Kolotuchin, S V -- GM39782/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1095-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Illinois, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599085" target="_blank"〉PubMed〈/a〉
    Keywords: Carboxylic Acids/*chemistry ; Chemistry, Physical ; Chromatography ; Hydrogen Bonding ; Macromolecular Substances ; Magnetic Resonance Spectroscopy ; Molecular Weight ; Physicochemical Phenomena ; Polymers/*chemical synthesis/chemistry ; Solvents
    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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  • 6
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    Role of phosphatidylinositol kinase in PDGF receptor signal transduction (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-03-03
    Description: The molecules with which the platelet-derived growth factor (PDGF) receptor interacts to elicit the biochemical reactions responsible for cell proliferation have not been identified. Antisera directed against specific PDGF receptor peptides coprecipitated a phosphatidylinositol (PI) kinase and the PDGF receptor. Immunoprecipitates from PDGF-stimulated cells contained 10 to 50 times as much PI kinase as those from unstimulated cells. Mutation of the PDGF receptor by deletion of its kinase insert region resulted in a receptor markedly less effective than the wild type in eliciting cell proliferation and defective in PDGF-stimulated PI kinase, but still capable of PDGF-induced receptor autophosphorylation and phosphoinositide hydrolysis. These data show that the PDGF receptor is physically associated with a PDGF-sensitive PI kinase that is distinct from tyrosine kinase and is not required for PDGF-induced PI hydrolysis. The finding that the mutant PDGF receptor missing the kinase insert domain elicited known early biochemical responses to PDGF, but did not associate with or regulate PI kinase, suggests a novel role for the receptor-associated PI kinase in the transmission of mitogenic signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coughlin, S R -- Escobedo, J A -- Williams, L T -- HL 32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Mar 3;243(4895):1191-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2466336" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Phosphatidylinositol 4-Kinase ; Animals ; Cell Line ; Chromatography ; Cricetinae ; Immunoassay ; Immunosorbent Techniques ; Mice ; Mice, Inbred BALB C ; Mutation ; Phosphatidylinositols/metabolism ; Phosphorylation ; Phosphotransferases/*metabolism ; Phosphotyrosine ; Platelet-Derived Growth Factor/pharmacology ; Protein-Tyrosine Kinases/metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Receptors, Platelet-Derived Growth Factor ; *Signal Transduction ; Tyrosine/analogs & derivatives/metabolism
    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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  • 7
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    Heterogeneity of vertebrate luteinizing hormone-releasing hormone (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-10-05
    Description: Radioimmunoassay and chromatography analyses of hypothalamic luteinizing hormone-releasing hormone (LHRH) have demonstrated the presence of LHRH-like immunoreactive peptides in a wide range of vertebrates. Contrary to previous reports, the molecule differs in various vertebrates. Avian, reptilian, and teleostean LHRH's are chemically distinct from the mammalian peptide but are in themselves indistinguishable. However, amphibian LHRH appears to be identical to the mammalian peptide. These findings have interesting evolutionary implications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, J A -- Millar, R P -- New York, N.Y. -- Science. 1979 Oct 5;206(4414):67-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/384514" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Chromatography ; Gonadotropin-Releasing Hormone/*analysis/immunology ; Hypothalamus/analysis ; Radioimmunoassay ; Species Specificity ; Structure-Activity Relationship
    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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  • 8
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    Contemporary methodology for protein structure determination (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-10-19
    Description: The techniques used for the characterization of protein and peptide structure have undergone great changes that have improved the speed, reliability, and applicability of the process. High-performance liquid chromatography and gel electrophoresis have made the purification of proteins and peptides a routine procedure, even when the compound of interest is a minor component of a complex biological mixture. The chemistry and instrumentation used in amino acid analysis and amino acid sequencing now permit the analysis of as little as 5 to 50 picomoles of samples. This represents an increase in sensitivity of more than a thousandfold over the last 10 years and has made possible the structural analysis of a wide variety of scarce but important compounds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunkapiller, M W -- Strickler, J E -- Wilson, K J -- New York, N.Y. -- Science. 1984 Oct 19;226(4672):304-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6385254" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Amino Acids/analysis ; Chemical Fractionation ; Chemistry Techniques, Analytical/*methods ; Chromatography ; Chromatography, High Pressure Liquid ; Chromatography, Ion Exchange ; Electrophoresis, Polyacrylamide Gel ; Isoelectric Focusing ; Peptide Hydrolases ; Peptides/analysis ; Proteins/*analysis/isolation & purification
    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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