Effects of N-acetylimidazole on oxytocin binding in bovine mammary tissue.
The effects of N-acetylimidazole on specific binding of oxytocin to microsomal fractions of bovine mammary gland were studied. N-acetylimidazole suppressed oxytocin binding, with time and concentration dependence. Decreased oxytocin binding activity appeared to be due to decreased affinity of the hormone for its receptor. Acetylation of oxytocin, rather than of oxytocin receptors, seemed to be responsible for the decreased binding.
Zhao
X
X
Department of Animal Science, New York State College of Agricultural and Life Sciences, Cornell University, Ithaca 14853.
Gorewit
R C
RC
Currie
W B
WB
D000107:Acetylation; D000818:Animals; D002417:Cattle; D004305:Dose-Response Relationship, Drug; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D007093:Imidazoles / Q000494:pharmacology*; D066298:In Vitro Techniques; D008321:Mammary Glands, Animal / Q000378:metabolism*; D010121:Oxytocin / Q000378:metabolism*; D011945:Receptors, Angiotensin / Q000378:metabolism*; D018045:Receptors, Oxytocin; D013057:Spectrum Analysis; D014316:Tritium
D006898:Hydroxylamines; D007093:Imidazoles; D011945:Receptors, Angiotensin; D018045:Receptors, Oxytocin; D014316:Tritium; D019811:Hydroxylamine; D010121:Oxytocin; C012160:N-acetylimidazole