Binding of N-(2-bromo ethyl)-N-ethyl-N 1 -naphthylmethylamine HBr (SY28) to the proteins of guinea-pig vas deferens.
1. Vasa deferentia from guinea-pigs were exposed to (14)C-SY28 HBr (5.32 x 10(-6)M) washed, lipid extracted, and broken up.2. The tissue was digested with papain, hydrolyzed with 6 N HCl, and gel filtration performed.3. Aliquots at each stage were used for paper chromatography and autoradiography.4. Three labelled spots (in addition to unbound 2-halogenoalkylamine) were located from acid hydrolysate and a fourth from gel filtrate.5. Selected amino-acids were complexed with (14)C-SY28 and the procedure repeated. The R(F) values were compared with those of the same amino-acids with and without 6 N HCl.6. Histidine, aspartic acid, arginine and serine gave a significant degree of binding of (14)C-SY28.7. The theoretical implications are discussed.
D000818:Animals; D001120:Arginine; D001224:Aspartic Acid; D001345:Autoradiography; D001665:Binding Sites; D002247:Carbon Isotopes; D002850:Chromatography, Gel; D002854:Chromatography, Paper; D005021:Ethylamines / Q000378:metabolism*; D006168:Guinea Pigs; D006639:Histidine; D066298:In Vitro Techniques; D008297:Male; D009281:Naphthalenes / Q000378:metabolism*; D011485:Protein Binding; D012694:Serine; D013565:Sympatholytics / Q000378:metabolism*; D014649:Vas Deferens / Q000378:metabolism*
D002247:Carbon Isotopes; D005021:Ethylamines; D009281:Naphthalenes; D013565:Sympatholytics; D001224:Aspartic Acid; D012694:Serine; D006639:Histidine; D001120:Arginine