Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Uwe Wollert"'
Publikováno v:
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology. 62:101-105
1. The stereospecificity of the interaction of the enantiomers of the anticoagulent drugs warfarin and phenprocoumon with bovine and rat serum albumin was investigated using equilibrium dialysis and circular dichroism measurements and compared with t
Publikováno v:
Naunyn-Schmiedeberg's Archives of Pharmacology. 319:172-177
Receptor binding studies were performed with tritiated propyl β-carboline-3-carboxylate ([3H]PrCC), tritiated ethyl β-carboline-3-carboxylate ([3H]ECC), and tritiated flunitrazepam ([3H]FNT) in membrane preparations from different regions of the bo
Autor:
Walter E. Müller, Uwe Wollert
Publikováno v:
Biochemical Pharmacology. 25:141-145
The binding of eleven benzodiazepine derivatives to bovine serum albumin was determined by means of Sephadex gel filtration. The albumin binding of the substances was characterized by the percentage of drug bound, the binding constants k + , K 1 , an
Autor:
Uwe Wollert, Walter E. Müller
Publikováno v:
Biochemical Pharmacology. 25:1459-1464
The interaction of four sulfonamides with bovine and human serum albumin (BSA and HSA) was investigated by means of circular dichroism and u.v. absorbance measurements. In the case of all sulfonamides, extrinsic Cotton effects could be found for the
Autor:
Hans Rommelspacher, Harald Borbe, Uwe Wollert, Walter E. Müller, Klaus J. Fehske, Christel Nanz
Publikováno v:
Naunyn-Schmiedeberg's Archives of Pharmacology. 314:97-100
The interaction of several beta-carbolines with specific [3H]-flunitrazepam binding to benzodiazepine receptors in rat brain membranes was investigated. Out of the investigated compounds, harmane and norharmane were the most potent inhibitors of spec
Publikováno v:
Neuroscience Letters. 9:239-243
Using [ 3 H]diazepam, benzodiazepine receptor binding has been investigated in rat spinal cord synaptosomal membranes. Specific [ 3 H]diazepam binding is saturable with a K D of about 8 nM and a maximal number of binding sites of 0.48 pmol/mg protein
Publikováno v:
Neuropharmacology. 19:121-124
The interaction of several central nervous system stimulating and depressing drugs with specific [3H]flunitrazepam binding to benzodiazepine receptors in rat brain membranes was investigated. Most of the investigated intravenous anesthetics, hypnotic
Autor:
Uwe Wollert, Walter E. Müller
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 427:465-480
The binding of suramin to bovine and human serum albumin was investigated by gel filtration and spectroscopic measurements. Besides some low-affinity binding sites suramin has, on the bovine serum albumin molecule one and on the human serum albumin m
Autor:
Walter E. Müller, Uwe Wollert
Publikováno v:
Pharmacology. 19:59-67
Most drugs are bound to human serum albumin (HSA) via a few high affinity binding sites and several sites of much lower affinity. There is now increasing evidence that the actual number of high affinity drug-binding sites of HSA is rather small. Thus
Autor:
Walter E. Müller, Uwe Wollert
Publikováno v:
Biochemical Pharmacology. 25:147-152
The interaction of benzodiazepine derivatives with bovine serum albumin (BSA) was studied by circular dichroism (CD) measurements. Most of the investigated benzoidiazepines show biphasic extrinsic Cotton effects, which are largely influenced by raisi