Burba J V
Can J Physiol Pharmacol. 1979 Feb;57(2):213-6. doi: 10.1139/y79-031.
Catechol O-methyltransferase (COMT) obtained from human liver (HL) and human placenta (HP) was found to be much less active than rat liver (RL) COMT when norepinephrine, epinephrine, dopamine, and isoproterenol are used as substrates. The Km values, which reflect the affinity of substrate and enzyme, show that RL COMT has the highest affinity toward the catecholamine substrates followed by HP COMT and then HL COMT. Both HP and RL COMT preparations O-methylate the catecholamines primarily in the meta position.
当以去甲肾上腺素、肾上腺素、多巴胺和异丙肾上腺素作为底物时,发现从人肝脏(HL)和人胎盘(HP)获得的儿茶酚-O-甲基转移酶(COMT)的活性远低于大鼠肝脏(RL)COMT。反映底物与酶亲和力的Km值表明,RL COMT对儿茶酚胺底物的亲和力最高,其次是HP COMT,然后是HL COMT。HP和RL COMT制剂都主要将儿茶酚胺甲基化在间位。