Newsome L R, Leitch G J
Digestion. 1978 Jul-Aug;17(4):370-3. doi: 10.1159/000198130.
Carbonic anhydrase (CA) was found to be equally susceptible to direct inhibition by ethanol, whether the enzyme originated from homogenates of rabbit gastric, duodenal, or ileal mucosa. When gastric mucosa was separated into a soluble (cytoplasmic) and a membrane fraction, the membrane CA was more susceptible to ethanol inhibition, but less susceptible to acetazolamide inhibition, than the soluble enzyme. Male rat liver CA is relatively insensitive to acetazolamide inhibition, while female rat liver CA shows a sensitivity similar to that of other tissues. We found ethanol inhibited male and female rat liver CA equally, indicating a different site, or mode, of inhibition for ethanol and acetazolamide.
结果发现，无论碳酸酐酶（CA）来源于兔胃、十二指肠或回肠黏膜的匀浆，其对乙醇的直接抑制作用均同样敏感。当将胃黏膜分离为可溶性（细胞质）组分和膜组分时，与可溶性酶相比，膜碳酸酐酶对乙醇抑制作用更敏感，但对乙酰唑胺抑制作用较不敏感。雄性大鼠肝脏碳酸酐酶对乙酰唑胺抑制作用相对不敏感，而雌性大鼠肝脏碳酸酐酶的敏感性与其他组织相似。我们发现乙醇对雄性和雌性大鼠肝脏碳酸酐酶的抑制作用相同，这表明乙醇和乙酰唑胺的抑制位点或方式不同。
