Abstract
Analysis by thin-layer chromatography showed that [ 14 C]N- acetyltryptamine and [ 14 C]N- acetyl-β- phenylethylamine are formed from the incubation of [ 14C]acetyl-CoA with tryptamine or β-phenylethylamine. respectively, in the presence of rat brain extracts. The specific activity of the N-acetyltransferase in fifteen discrete regions of rat CNS ranged from 1.64 ± 0.05 nmoles of product formed/mg of protein/hr in cerebellum to 0.57 ± 0.05 nmole in occipital cortex with tryptamine as substrate, and from 2.80 ± 0.30 nmoles in cerebellum to 0.91 ± 0.13 nmole in cervical cord with β- phenylethylamine as substrate. Comparison of the regional specific activities in the presence of the respective substrates yielded a correlation coefficient of 0.83 (P < 0.01). In cerebellum N-acetyltransferase activity appears exclusively in cytosol. At two stages of purification (i.e. after Bio-Gel fractionation as well as after ammonium sulfate precipitation), the enzyme exhibited biphasic kinetics with respect to acetyl-CoA in the presence of tryptamine or β-phenylelhylamine and with respect to either substrate in the presence of acetyl-CoA.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
