Pendleton R G, Gessner G, Sawyer J
Naunyn Schmiedebergs Arch Pharmacol. 1980 Sep;313(3):263-8. doi: 10.1007/BF00505743.
Phenylethanolamine N-methyltransferase (PNMT) was identified as the primary, high affinity N-methylating enzyme for phenylethanolamine (PEA) in rat, dog and Rhesus monkey lung. Human and rabbit lung, however, do not contain this enzyme but possess a more non-specific or general N-methyltransferase with a relatively low affinity for PEA and for which beta-phenethylamine (beta-PE) is also a substrate. The former but not the latter enzyme is markedly inhibited by micromolar concentrations of the PNMT antagonist, SK & F 64139. This evidence indicates that certain species differences exist for the enzyme system(s) available for the N-methylation of phenethylamine-type compounds in pulmonary tissue.
苯乙醇胺N-甲基转移酶(PNMT)被确定为大鼠、狗和恒河猴肺中苯乙醇胺(PEA)的主要高亲和力N-甲基化酶。然而,人和兔的肺中不含有这种酶,而是具有一种对PEA亲和力相对较低的更非特异性或通用的N-甲基转移酶,β-苯乙胺(β-PE)也是该酶的底物。前者而非后者的酶会被微摩尔浓度的PNMT拮抗剂SK & F 64139显著抑制。这一证据表明,肺组织中用于苯乙胺类化合物N-甲基化的酶系统存在某些物种差异。