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  • D-Cysteinolic acid  (1)
  • Itraconazole  (1)
  • Key words. Cadmium; cysteine; Escherichia coli; expression; metal; amino acid replacement; α-fragment; metallothionein.  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Cellular and molecular life sciences 53 (1997), S. 459-465 
    ISSN: 1420-9071
    Schlagwort(e): Key words. Cadmium; cysteine; Escherichia coli; expression; metal; amino acid replacement; α-fragment; metallothionein.
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Abstract. To evaluate whether only 20 cysteine residues at invariant positions are needed to bind and coordinate the metals in metallothioneins (MTs), and whether changing the positions of cysteine residues in the sequence affects the metal-binding capacity and the coordination of MTs, we examined the cadmium-binding affinities of seven mutant MTαs using an Escherichia coli expression system. Five mutant MTαs in which the constitutive amino acid residues other than cysteines of the α-fragment were replaced with glycine residues, and the remaining two mutant MTαs in which the invariant positions of the cysteine residues of the α-fragment were shifted, were analysed for their ability to be expressed as cadmium-binding forms and for their biochemical properties. The results showed that extreme alteration of the constitutive amino acid residues other than cysteines in the MT α-fragment leads to disruption of their cadmium-binding abilities and of their structure. However, mutant MTαs containing changes of the invariant positions of the cysteine residues were expressed in a cadmium-binding form in Escherichia coli, although the invariant positions of 20 cysteine residues in the MTs are thought to be important for their metal-binding abilities. These results suggest that the position of cysteine residues and the chemical nature of the other amino acids in the amino acid sequence of MTs are less critical than expected.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Cellular and molecular life sciences 45 (1989), S. 1110-1112 
    ISSN: 1420-9071
    Schlagwort(e): D-Cysteinolic acid ; platelet aggregation ; inhibitor ; marine product ; 2-aminoethyl disulfide ; sardine
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary D-Cysteinolic acid (1) analogues with an S-C-C-N skeleton showed increased platelet anti-aggregant activity in the following order: 2-aminoethanesulfonic acids, thiazolidines, 2-aminoethanethiols and 2-aminoethyl disulfides. Methyl substitutions at the 2-position potentiated the activity. Of these analogues, bis [(R)-2-aminopropyl] disulfide was the most potent inhibitor of platelet aggregation, with about 600-fold the activity of (1).
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    ISSN: 1432-0584
    Schlagwort(e): Key words Multidrug resistance ; P-glycoprotein ; Itraconazole ; Adriamycin ; Etoposide
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract  Itraconazole is a triazole antifungal agent that inhibits cell membrane serol biosynthesis. Currently, itraconazole is a potent candidate for in vivouse to revert multidrug resistance in acute leukemias, with the added benefit of its antifungal effect. As previously reported, itraconazole, as well as verapamil, reversed adriamycin-resistant K562 cells (K562/ADR) and HL60 cells (HL60/ADR) in dosages compatible to the plasma levels achieved by the therapeutic dosages used for the treatment of fungal infections. By RT-PCR analysis of mdr1, mdr3, and mrp mRNA, these adriamycin-resistant cells showed a higher expression of the transcript of these genes than those of the parent cells. By FACS analysis, both the adriamycin-resistant cells showed a higher expression of P-glycoprotein on their cell surfaces. These results suggested the involvement of itraconazole in the mdr gene and/or mrp gene product-associated resistance. Furthermore, itraconazole partially reversed etoposide resistance in both the K562 and K562/ADR cells. The present study suggests that itraconazole may reverse multidrug resistance, at least in part, via a classical MDR-associated mechanism.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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