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  • 1
    Digitale Medien
    Digitale Medien
    Rooting, growth and ethylene evolution of pea cuttings in response to chloroindole auxins (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 69 (1987), S. 0 
    Details
    ISSN: 1399-3054
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: In pea cuttings (Pisum sativum L. cv. Alaska) we measured shoot and root growth and ethylene production in response to 4-chloroindole-3-acetic acid (4-CI-IAA) or 4,6-dichloroindole-3-acetic acid (4,6-Cl2-IAA). Leafy cuttings treated basally with either of the chlorinated auxins in high concentrations showed permanent epinasty, loss of apical growth and dominance resulting in the outgrowth of laterals from the lower-most axillary bud. The naturally occurring 4-CI-IAA was a better root promoter than the synthetic 4,6-Cl2-IAA which inhibited rooting. Both chloroindole auxins induced very high ethylene evolution, which lasted much longer than the ethylene evolution after IAA treatment.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1399-3054.1987.tb01956.x
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Soluble, fatty acid acylated insulins bind to albumin and show protracted action in pigs (1996)
    Springer
    Diabetologia 39 (1996), S. 281-288 
    Details
    ISSN: 1432-0428
    Schlagwort(e): Insulin analogues ; albumin binding ; prolonged action ; basal insulin ; fatty acids ; tetradecanoic acid ; myristic acid ; lysineB29 ; acylation ; receptor affinity
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary We have synthesized insulins acylated by fatty acids in the ε-amino group of LysB29. Soluble preparations can be made in the usual concentration of 600 nmol/ml (100 IU/ml) at neutral pH. The time for 50% disappearance after subcutaneous injection of the corresponding TyrA14(125I)-labelled insulins in pigs correlated with the affinity for binding to albumin (r=0.97), suggesting that the mechanism of prolonged disappearance is binding to albumin in subcutis. Most protracted was LysB29-tetradecanoyl des-(B30) insulin. The time for 50% disappearance was 14.3±2.2 h, significantly longer than that of Neutral Protamine Hagedorn (NPH) insulin, 10.5±4.3 h (p〈0.001), and with less inter-pig variation (p〈0.001). Intravenous bolus injections of LysB29-tetradecanoyl des-(B30) human insulin showed a protracted blood glucose lowering effect compared to that of human insulin. The relative affinity of LysB29-tetradecanoyl des-(B30) insulin to the insulin receptor is 46%. In a 24-h glucose clamp study in pigs the total glucose consumptions for LysB29-tetradecanoyl des-(B30) insulin and NPH were not significantly different (p=0.88), whereas the times when 50% of the total glucose had been infused were significantly different, 7.9±1.0 h and 6.2±1.3 h, respectively (p〈0.04). The glucose disposal curve caused by LysB29-tetradecanoyl des-(B30) insulin was more steady than that caused by NPH, without the pronounced peak at 3 h. Unlike the crystalline insulins, the soluble LysB29-tetradecanoyl des-(B30) insulin does not elicit invasion of macrophages at the site of injection. Thus, LysB29-tetradecanoyl des-(B30) insulin might be suitable for providing basal insulin in the treatment of diabetes mellitus.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00418343
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Soluble, fatty acid acylated insulins bind to albumin and show protracted action in pigs (1996)
    Springer
    Diabetologia 39 (1996), S. 281-288 
    Details
    ISSN: 1432-0428
    Schlagwort(e): Keywords Insulin analogues ; albumin binding ; prolonged action ; basal insulin ; fatty acids ; tetradecanoic acid ; myristic acid ; lysineB29 ; acylation ; receptor affinity.
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary We have synthesized insulins acylated by fatty acids in the ɛ-amino group of LysB29. Soluble preparations can be made in the usual concentration of 600 nmol/ml (100 IU/ml) at neutral pH. The time for 50 % disappearance after subcutaneous injection of the corresponding TyrA14(125I)-labelled insulins in pigs correlated with the affinity for binding to albumin (r = 0.97), suggesting that the mechanism of prolonged disappearance is binding to albumin in subcutis. Most protracted was LysB29-tetradecanoyl des-(B30) insulin. The time for 50 % disappearance was 14.3 ± 2.2 h, significantly longer than that of Neutral Protamine Hagedorn (NPH) insulin, 10.5 ± 4.3 h (p 〈 0.001), and with less inter-pig variation (p 〈 0.001). Intravenous bolus injections of LysB29-tetradecanoyl des-(B30) human insulin showed a protracted blood glucose lowering effect compared to that of human insulin. The relative affinity of LysB29-tetradecanoyl des-(B30) insulin to the insulin receptor is 46 %. In a 24-h glucose clamp study in pigs the total glucose consumptions for LysB29-tetradecanoyl des-(B30) insulin and NPH were not significantly different (p = 0.88), whereas the times when 50 % of the total glucose had been infused were significantly different, 7.9 ± 1.0 h and 6.2 ± 1.3 h, respectively (p 〈 0.04). The glucose disposal curve caused by LysB29-tetradecanoyl des-(B30) insulin was more steady than that caused by NPH, without the pronounced peak at 3 h. Unlike the crystalline insulins, the soluble LysB29-tetradecanoyl des-(B30) insulin does not elicit invasion of macrophages at the site of injection. Thus, LysB29-tetradecanoyl des-(B30) insulin might be suitable for providing basal insulin in the treatment of diabetes mellitus. [Diabetologia (1996) 39: 281–288]
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00418343
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