Gessler N N, Fedotcheva N I, Foĭgel' A G, Alekseeva N V, Kondrashova M N, Bykhovskiĭ V Ia
Biokhimiia. 1995 Jun;60(6):981-6.
Changes in the activity of monoamine oxidase (MAO-B) in liver homogenates and mitochondria from normal and vitamin B12-deficient rats have been studied in various functional states of the mitochondria. Preincubation of liver preparation at 32 degrees C increased the MAO affinity for benzylamine in samples of normal (but not vitamin B12-deficient rats). Succinate added to the incubation medium decreased Km and increased Vmax in both normal and vitamin B12-deficient animals. A correlation was found between the decline of MAO-B activity under vitamin B12 deficiency, deceleration of succinate oxidation and reduction of the transmembrane potential.
研究了正常和维生素B12缺乏大鼠肝脏匀浆和线粒体中,单胺氧化酶(MAO-B)活性在各种线粒体功能状态下的变化。在32℃对肝脏制剂进行预孵育,增加了正常大鼠(而非维生素B12缺乏大鼠)样本中MAO对苄胺的亲和力。向孵育培养基中添加琥珀酸,降低了正常和维生素B12缺乏动物的Km并增加了Vmax。发现维生素B12缺乏时MAO-B活性下降、琥珀酸氧化减速和跨膜电位降低之间存在相关性。