Ambroziak W, Maśliński C
Department of Biogenic Amines, Polish Academy of Sciences, Lódź.
Agents Actions. 1988 Apr;23(3-4):311-3. doi: 10.1007/BF02142573.
Some guinea pig tissue homogenates have shown the ability to catabolize, in vitro, imidazoloacetaldehyde (ImAAL) and gamma-aminobutyraldehyde (GABAL) via NAD-dependent aldehyde dehydrogenase (ALDH, EC 1.2.1.3). The liver, kidney, small intestine and gastric mucosa are the richest sources of ALDH activity towards ImAAL. The liver, kidney, small intestine and pancreas also show ALDH activity with GABAL as a substrate. All tissues tested have shown low Km and high Km ALDH activity with propionaldehyde as substrate. The guinea pig liver ALDH which is able to oxidize ImAAL and GABAL is located exclusively in the cytoplasm.
一些豚鼠组织匀浆已显示出在体外通过NAD依赖性醛脱氢酶(ALDH,EC 1.2.1.3)分解代谢咪唑乙醛(ImAAL)和γ-氨基丁醛(GABAL)的能力。肝脏、肾脏、小肠和胃黏膜是对ImAAL具有最高ALDH活性的来源。肝脏、肾脏、小肠和胰腺也显示出以GABAL为底物的ALDH活性。所有测试组织均显示出以丙醛为底物的低Km和高Km ALDH活性。能够氧化ImAAL和GABAL的豚鼠肝脏ALDH仅位于细胞质中。