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  • 1
    Electronic Resource
    Electronic Resource
    A new hybrid resin for stepwise screening of peptide libraries combined with single bead Edman sequencing (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 282-288 
    Details
    ISSN: 1075-2617
    Keywords: Synthetic peptide library ; one-bead-one-compound ; partial cleavage ; soluble phase screening ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A library system was developed for the discovery of bioactive peptides. Library synthesis and peptide sequencing was performed on a solid support while the screening for bioactivity was done with peptides in solution. The peptides were synthesized by split and mix, one-bead-one-peptide library synthesis, using a Tentagel S-NH2 solid support with a loading of approximately 100 pmol/bead. The major part of the peptide was connected to the support by a single acid-labile linker and a minor part of the peptide was acid-stabile attached to the polymer. The percentage of acid-stabile attached peptides could easily be controlled during modification of the amino functionalities of the resin at the start of the process. The cleavage rate of the acid-labile attached peptide from the resin depends on the composition of the cleavage mixture. When cleavage conditions were carefully controlled, a three-step partial cleavage protocol allowed for convergent bioactivity screening on peptide libraries using only one type of acid-labile linker. The partial cleavage and convergent screening procedure was repeated three times, after which the bead containing the bioactive peptide was sequenced. As such a bead still contained acid-stabile attached peptide, the Edman sequencing was straightforward and repetitive yields were excellent because the immobilized peptide was not washed out. © 1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 2
    Electronic Resource
    Electronic Resource
    Experimental conditions influence [3H]-dihydroalprenolol binding characteristics to living HeLa cells due to morphological changes: A warning (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 5 (1987), S. 143-147 
    Details
    ISSN: 0263-6484
    Keywords: Radioligand binding ; HeLa cells ; beta-adrenergic receptor ; cell morphology ; non-specific binding ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Harvesting of plated growing HeLa cells, followed by incubation of these cells without any addition at 37°C was found to cause changes in the cell shape. This phenomenon is accompanied by a diminished binding of the beta-adrenergic antagonist [3H]-dihydroalprenolol and the alpha-adrenergic antagonist phentolamine to a binding compartment not representing beta-adrenergic receptors. These binding sites have a high affinity for hydrophobic agents and most probably represent lipophilic structures in the cellular membrane. Changes in the cell shape obviously cause alterations in the physical properties of the plasma membrane. This might lead to misinterpretations of the results from experiments in which the redistribution of beta-adrenergic receptors is followed during incubation with agonists, as receptor occupation with subsequent receptor redistribution is possibly accompanied by effects on the membrane microviscosity.It is concluded that investigations performed in order to follow physiological events like receptor redistribution and desensitization processes, may be obfuscated by changes in the normal physical state of the living cells.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290050210
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  • 3
    Electronic Resource
    Electronic Resource
    The preparative isolation of endosome fractions: A review (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 5 (1987), S. 235-243 
    Details
    ISSN: 0263-6484
    Keywords: Endocytosis ; endosomes ; polymeric IgA, transcytosis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The endosome is an intracellular, acidic, membrane-bound, subcellular compartment to which endocytosed ligands, receptors and plasma membrane proteins are conveyed before sorting and delivery to destinations elsewhere in the cell. The preparative isolation of elements of this compartment has been achieved successfully using various appropriate combinations of density gradient ultracentrifugation, electrophoretic, gel filtration and immunoaffinity techniques. These methods for isolating endosome fractions are reviewed together with the difficulties of establishing markers for such fractions. The isolation of an endosome fraction from the pathway of polymeric IgA transcytosis in rat liver is discussed to exemplify successful isolation procedures and appropriate subcellular markers.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290050402
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