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1979 (1)
1974 (1)
1Author    Ralf Janda, Gert HellerRequires cookie*
 Title    1 B—NMR-spektroskopische Untersuchungen an wäßrigen Polyboratlösungen n B NMR Spectroscopic Studies on Aqueous Polyborate Solutions  
 Abstract    The U B nuclear magnetic resonance spectra of sodium, potassium and ammonium polyborates in aqueous solutions, -as a function of concentration and pH -, provide information of the hydrolysis equilibria. Two n B NMR lines are observed in aqueous solutions of Na[B506(0H)4], K[B506(0H)4] and NH4[B506(0H)4]. Only one n B NMR line is recorded in aqueous solutions of (NH4)2[B4Os(OH)4] and Na2[B4Os(OH)4]. The results of the U B NMR spectra are discussed and compared with the results obtained from Raman studies of aqueous polyborate solutions. 
  Reference    Z. Naturforsch. 34b, 1078—1083 (1979); eingegangen am 13. März/27. April 1979 
  Published    1979 
  Keywords    n B NMR, Borates, Polyborates, Hydrolysis, Equilibria 
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 TEI-XML for    default:Reihe_B/34/ZNB-1979-34b-1078.pdf 
 Identifier    ZNB-1979-34b-1078 
 Volume    34 
2Author    Richard Wahl, Ekkehard KalleeRequires cookie*
 Title    Einfluß verschiedener Medikamente auf die Bindung von Schilddrüsenhormonen an Lebermitochondrien Influence of Various Drugs on the Adsorption of Thyroid Hormones to Liver Mitochondria  
 Abstract    Distribution 1. [131I] L-thyroxine (T4) or [131I]L-triiodothyronine (T3) was added in 50 pM — 25 nM and 26 pM —132 nM concentrations to suspensions of rat liver mitochondria. In distribution equilibria between soluble proteins and mitochondria the adsorption of the thyroid hormones to the mito­ chondria followed an approximately linear function when the radioactive hormones were added within the range of physiological concentrations. At identical protein concentrations T3 was ad­ sorbed to the mitochondria one tenth more strongly than T4 when neither serum proteins nor cell sap had been added. The adsorption of both T3 and T4 to mitochondria and soluble proteins is reversible. The distribution of the thyroid hormones between organelles and soluble proteins depends on the ratio of the protein concentration in the sedimented mitochondria to the protein concentration in the supernate after centrifugation. The desorption of T3 and T4 from the mito­ chondria by soluble proteins, however, represents no linear function. 2. The distribution equilibria of simultaneously added 131I —T4 and 125I —T3 can be shifted by certain drugs. Chlorpromazin and dinitrophenol displaced the thyroid hormones from their binding to soluble proteins onto the mitochondria. Vice versa, phenylbutazone, phenytoin, brom-sulfalein and silymarin displaced the hormones from the mitochondria more strongly than from soluble proteins. Sodium oleate displaced the hormones in both directions. Minor shifting effects or none at all could be detected when several other drugs were used. The described procedure apparently yields new information on some effects of drug action. 
  Reference    (Z. Naturforsch. 29c, 608 [1974]; eingegangen am 14. Mai 1974) 
  Published    1974 
  Keywords    Equilibria, Drug Action, Mitochondria, Protein Binding, Thyroid Hormones 
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 TEI-XML for    default:Reihe_C/29/ZNC-1974-29c-0608.pdf 
 Identifier    ZNC-1974-29c-0608 
 Volume    29