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  • 1
    Electronic Resource
    Electronic Resource
    Immobilization of tyrosinase within polyacrylamide gels (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 1405-1412 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The enzyme tyrosinase (E.G. 1.14.18.1) has been immobilized in a polyacrylamide gel and intermittently assayed for enzyme activity over a period of 19 days using phenol as the substrate. The results of these studies indicate that the immobilized enzyme could be incorporated into a system to detect phenol and related compounds that are found in industrial effluents and as surface water contaminants.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260181007
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  • 2
    Electronic Resource
    Electronic Resource
    Immobilization of nitrate reductase within polyacrylamide gels (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 1643-1645 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260181115
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  • 3
    Electronic Resource
    Electronic Resource
    Role of platinum black in a bio-fuel cell using glucose or hydrogen as fuel source (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 1687-1689 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260201016
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  • 4
    Electronic Resource
    Electronic Resource
    Potentiometric method for subatrate analysis using immobilized NAD+-dependent oxidoreductase enzymes (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 1905-1915 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Two coenzyme-dependent oxidoreductases, glucose dehydrogenase and alcohol dehydrogenase, were immobilized in polyacrylamide gel over a platinum grid matrix and used as enzyme electrodes to measure their substrate concentrations in buffered aqueous solutions. The immobilized enzymes were used to oxidize their substrates in the presence of NAD+. Ferricyanide was used as the redox mediator and electroactive specific. The determinations of glucose and ethenol were utilized to demonstrate and evaluate the performance of the system. The described methodology should be readily applicable to the analysis of numerous other substrates of coenzyme-dependent oxidoreductases.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260211103
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  • 5
    Electronic Resource
    Electronic Resource
    Synthesis of a novel side-chain to side-chain cyclized enkephalin analogue containing a carbonyl bridge (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 3 (1997), S. 277-281 
    Details
    ISSN: 1075-2617
    Keywords: cyclic opioid peptide analogue ; side-chain to side-chain cyclized peptides ; solid-phase peptide synthesis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A novel type of cyclic opiod peptide analogue, cyclo(N∊,N∊′-carbonyl- D-Lys2,Lys5)enkephalinamide, was prepared from a linear precursor peptide. The peptide was synthesized on the Merrifield resin and also by a combination of the solid-phase technique and the classical method in solution. In both cases the cyclization was performed by reaction of bis(4-nitrophenyl)carbonate with the free side-chain amino groups of the two lysine residues. The described method permits the convenient preparation of novel peptide analogues cyclized via a ureido group incorporating the side-chain amino groups of two α,ω-diamino acid residues. The cyclic enkephalin analogue containing a 21-membered ring structure showed preference for μ over δ opioid receptors in opioid bioassays in vitro. © 1997 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Synthesis and bioactivity studies of 1-adamantanamine derivatives of peptides (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 303-310 
    Details
    ISSN: 1075-2617
    Keywords: 1-Adamantanamine ; peptide synthesis ; opioid compounds ; antiviral agents ; HIV-1 ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Small enkephalin-related peptides containing a 1-adamantanamine moiety coupled through an amide linkage at the C-terminus were synthesized. Several of the compounds showed high μ opioid activity and μ receptor selectivity. The new adamantanamine derivatives were also examined for antiviral activity against HIV-1 in a cell culture system. Some of them inhibited syncytia formation even when the antigen assay gave evidence for viral replication.
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010505
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  • 7
    Electronic Resource
    Electronic Resource
    Enkephalin analogs containing 4,4-difluoro-2-aminobutyric acid: Synthesis and fluorine effect on the biological activity (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 496-501 
    Details
    ISSN: 1075-2617
    Keywords: enkephalins ; DPDPE ; opioid agonists ; δ-receptor ; fluorine containing amino acid ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Analogs of Met-enkephalin and [d-Pen2, d-Pen5]enkephalin (DPDPE) containing the partially fluorinated amino acid 4,4-difluoro-2-aminobutyric acid (DFAB) in the 2- or 3-position of the peptide sequence were synthesized and their opioid activities and receptor selectivities were determined in vitro. The linear fluorinated [d-DFAB2, Met5-NH2]enkephalin showed μ and δ agonist potencies comparable to those of natural [Leu5]enkephalin. The partially fluorinated DPDPE analogs behaved differently as compared with their non-fluorinated correlates. While l-amino acid substitution in position 3 of DPDPE usually resulted in higher δ agonist potency than d-amino acid substitution, [d-DFAB3]DPDPE turned out to be a more potent δ agonist than [l-DFAB3]DPDPE. Furthermore, [d-DFAB3]DPDPE showed over 100-fold higher δ agonist potency than [d-Abu3]DPDPE (Abu=2-aminobutyric acid), indicating that the fluorine substituents interact favorably with a δ opioid receptor subsite. © 1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Highly potent side chain-main chain cyclized dermorphin-deltorphin analogues: An integrated approach including synthesis, bioassays, NMR spectroscopy and molecular modelling (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 157-174 
    Details
    ISSN: 1075-2617
    Keywords: Opioid bioactivities ; bioactive conformations ; NMR studies ; molecular modelling ; synthesis of cyclic opioids ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Our continuing efforts to study structure-activity relationships of peptide opioids have resulted in the synthesis of a series of cyclic opioids related to dermorphins and deltorphins. The biological activities of the compounds have been determined and the conformational analyses carried out using 1H-NMR spectroscopy and molecular modelling. The three compounds in the series Tyr-c[D-Orn-Phe-Ala], Tyr-c[D-Lys-Phe-Ala], and Tyr-c[A2Bu-Phe-Ala-Leu] are cyclized via a lactam bridge from the side-chain of the residue at the second position with the carboxyl terminus of each compound. The molecules incorporate 12-, 13- and 14-membered rings, respectively. They include a phenylalanine at the third position which is a distinguishing characteristic of dermorphins and deltorphins. The guinea pig ileum and mouse vas deferens assays show that the compounds are highly active at both μ- and δ-opioid receptors. The compounds are all highly effective antinociceptive agents as measured by the intrathecal rat hot plate test. Conformational analyses of the molecules indicate that they can adopt topochemical arrays required for bioactivity at both μ- and δ-receptors which explains their high activity in both guinea pig ileum and mouse vas deferens in vitro assays. The results support our models for μ- and δ-receptor activity for constrained peptide opioids.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010303
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