Estonian
Albanian
Arabic
Armenian
Azerbaijani
Belarusian
Bengali
Bosnian
Catalan
Czech
Danish
Deutsch
Dutch
English
Estonian
Finnish
Français
Greek
Haitian Creole
Hebrew
Hindi
Hungarian
Icelandic
Indonesian
Irish
Italian
Japanese
Korean
Latvian
Lithuanian
Macedonian
Mongolian
Norwegian
Persian
Polish
Portuguese
Romanian
Russian
Serbian
Slovak
Slovenian
Spanish
Swahili
Swedish
Turkish
Ukrainian
Vietnamese
Български
中文(简体)
中文(繁體)
Biochemical Pharmacology 1986-Oct

Heterogeneity between soluble human and rabbit splenic alpha 2-adrenoceptors.

Ainult registreeritud kasutajad saavad artikleid tõlkida
Logi sisse
Link salvestatakse lõikelauale
R M McKernan
K E Dickinson
C M Miles
P S Sever

Märksõnad

Abstraktne

The pharmacological and biochemical characteristics of soluble alpha 2-adrenoceptors were investigated to determine whether differences observed in membranes were maintained in solution and to probe the nature of any such differences. alpha 2-Adrenoceptors were solubilized from purified plasma membrane preparations of human and rabbit spleen using digitonin. [3H]yohimbine bound to one population of alpha 2-adrenoceptors in the preparations with dissociation constants of 2.4 nM and 7.8 nM respectively. The pharmacological profile of the alpha 2-adrenoceptors has been examined. Upon solubilization the affinity of the alpha 2-adrenoceptors for yohimbine was unchanged. In contrast, the potency of idazoxan and RX 811066 were increased, whereas the potency for prazosin (human only), phentolamine and WY 26392 was decreased 2-3-fold. The potency of the agonists oxymetazoline, UK 14304 and adrenaline were all reduced upon solubilization of alpha 2-adrenoceptors. The selectivity of yohimbine, idazoxan, RX 811066 and WY 26392 for human rather than rabbit alpha 2-adrenoceptors was maintained in solution. Possible sources of heterogeneity between human and rabbit alpha 2-adrenoceptors were investigated. The protein structure was probed by comparing the susceptibility of the receptors to inactivation by sulphydryl modifying agents. No differences were observed in the potency of N-ethylmaleimide or p-chloromercuribenzoate to inactivate the receptor. The carbohydrate component of the receptors was investigated using agarose-linked lectins. Rabbit splenic alpha 2-adrenoceptors had a lower affinity for the lectins wheatgerm agglutinin (Triticum vulgaris) and soybean (Glycine max) which bind the sugars N-acetyl d-glucosamine and N-acetyl d-galactosamine respectively. These findings suggest that heterogeneity of the alpha 2-adrenoceptor derives from its structural characteristics rather than its environment in the membrane.

Liitu meie
facebooki lehega

Kõige täiuslikum ravimtaimede andmebaas, mida toetab teadus

  • Töötab 55 keeles
  • Taimsed ravimid, mida toetab teadus
  • Maitsetaimede äratundmine pildi järgi
  • Interaktiivne GPS-kaart - märgistage ürdid asukohas (varsti)
  • Lugege oma otsinguga seotud teaduspublikatsioone
  • Otsige ravimtaimi nende mõju järgi
  • Korraldage oma huvisid ja hoidke end kursis uudisteuuringute, kliiniliste uuringute ja patentidega

Sisestage sümptom või haigus ja lugege ravimtaimede kohta, mis võivad aidata, tippige ürdi ja vaadake haigusi ja sümptomeid, mille vastu seda kasutatakse.
* Kogu teave põhineb avaldatud teaduslikel uuringutel

Google Play badgeApp Store badge