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  • 1985-1989  (2)
  • Binding site (ethylene)
  • hypertension
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    European journal of clinical pharmacology 29 (1985), S. 33-36 
    ISSN: 1432-1041
    Schlagwort(e): cold sensitivity ; hypertension ; alpha- and beta-blockade
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie , Medizin
    Notizen: Summary The presence of cold sensitivity was investigated in three groups of patients; untreated hypertensives and hypertensives treated by a beta-adrenoceptor blocker (propranolol) or by a combined alpha-and beta-adrenoceptor blocker (labetalol) at two ambient temperatures. At a comfortable ambient (24°C) one-third of the untreated and those treated with beta-blockade only showed cold sensitivity as compared with 16% of patients on the combined therapy. Under conditions of mild cold stress (20°C) cold sensitivity increased in frequency in all three groups, more than half of the untreated and beta-blocked patients were affected and greater than one-third of those with alpha- and beta-blockade. These findings indicate that in the general population of hypertensives treatment with beta-adrenoceptor blockade alone may have little effect on the peripheral vasculature and that a useful degree of protection may be provided by therapy which blocks both receptors.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Planta 164 (1985), S. 272-277 
    ISSN: 1432-2048
    Schlagwort(e): Binding site (ethylene) ; Ethylene (binding site) ; Phaseolus (ethylene binding)
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The solubilised ethylene-binding site (EBS) of Phaseolus vulgaris L. cotyledons is an asymmetrical protein with a sedimentation coefficient of 2 S and a Stoke's radius of 6.1 nm (determined by ultracentrifugation on isokinetic gradients and gel-permeation chromatography, respectively). The molecular weight and frictional ratio were calculated as 52 000–60 000 and 2.37–2.48, respectively. The EBS has an isoelectric point at between pH 3–5, determined by isoelectric focussing and exhibits a negative charge at pH 8 during non-denaturing electrophoresis. The electrical charge on the EBS is shielded; the EBS does not bind to anion-exchange media under the experimental conditions reported here, is not precipitated by ammonium sulphate and does not precipitate at its isoelectric pH. The EBS preferentially partitions into detergent phases. The results indicate that the EBS is a hydrophobic protein complexed with detergent in aqueous solution. The techniques used to characterise the EBS also resulted in varying degress of purification.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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