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Characterization of kappa1 and kappa2 opioid binding sites in frog (rana esculenta) brain membrane preparation (1990)

Benyhe, Sandor ; Varga, Eva ; Hepp, Jozsef ; [et al.]

Springer

Neurochemical research 15 (1990), S. 899-904

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ISSN: 1573-6903

Keywords: Opioid receptor subtypes ; frog brain ; kappa receptors ; equibibrium binding experiments ; [3H]ethylketocyclazocine

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract The distribution and properties of frog brain kappa-opioid receptor subtypes differ not only from those of the guinea pig brain, but also from that of the rat brain. In guinea pig cerebellum the kappa1 is the dominat receptor subtype, frog brain contains mainly the kappa2 subtype, and the distribution of the rat brain subtypes is intermediate between the two others. In competition experiments it has been established that ethylketocyclazocine and N-cyclopropylmethyl-norazidomorphine, which are nonselective kappa-ligands, have relatively high affinities to frog brain membranes. The kappa2 ligands (Met5)enkephalin-Arg6-Phe7 and etorphine also show high affinities to the frog brain. Kappa1 binding sites measured in the presence of 5 μM /D-Ala2-Leu5/enkephalin represent 25–30% of [3H]ethylketocyclazocine binding in frog brain membranes. The kappa2 subtype in frog brain resembles more to the mu subtype than the delta subtype of opioid receptors, but it differs from the mu subtype in displaying low affinity toward beta-endorphin and /D-Ala2-(Me)Phe4-Gly5-ol/enkephalin (DAGO). From our data it is evident that the opioid receptor subtypes are already present in the amphibian brain but the differences among them are less pronounced than in mammalian brain.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00965909

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Stereoselective effect of warfarin and bilirubin on the binding of 5-(o-chlorophenyl)-1,3-dihydro-3-methyl-7-nitro-2H-1,4- benzodiazin-2-one enantiomers to human serum albumin (1990)

Fitos, Ilona ; Visy, Julia ; Magyar, Anna ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Chirality 2 (1990), S. 161-166

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ISSN: 0899-0042

Keywords: protein binding ; affinity chromatography ; resolution ; allosteric interaction ; increased enantioselectivity ; Chemistry ; Organic Chemistry

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: The binding of the title benzodiazepine enantiomers and its modulation by warfarin and bilirubin were studied by chromatography on human serum albumin (HSA) immobilized on Sepharose 4B, and also by a combination of ultrafiltration and circular dichroism (UF-CD) methods. In the absence of warfarin and bilirubin the binding of the benzodiazepine was not stereoselective. (S)-Benzodiazepine and (S)-warfarin mutually increased the binding of each other, while the binding of (R)-benzodiazepine was preferentially enhanced on HSA saturated with bilirubin.

Additional Material: 4 Ill.