Kint J A, Dacremont G, Carton D, Orye E, Hooft C
Science. 1973 Jul 27;181(4097):352-4. doi: 10.1126/science.181.4097.352.
Total activities of acid hydrolases in liver of two patients with mucopolysaccharidosis are decreased for beta-galactosidase, alpha-galactosidase, and arylsulfatase A; total activities of four other hydrolases are normal or increased. The isoenzyme distribution of five hydrolases (beta-glucuronidase, alpha-glucosidase, beta- galactosidase, N-acetyl-beta-glucosaminidase, and alpha-galactosidase) is ábnormal in that the isoelectric points (by isoelectric focusing) of these enzymes are more acid than in control liver. Along with the isoenzyme abnormalities different kinds of glycolipids were stored in kidney, liver, and brain. The isoenzyme abnormalities can be reproduced in vitro by addition of chondroitin sulfate to a homogenate of normal liver, suggesting that stable binding occurs between mucopolysaccharides and the hydrolase molecules. After the addition of chondroitin sulfate, the total activity of beta-galactosidase is inhibited, whereas other hydrolases are affected only slightly or not at all.
两名黏多糖贮积症患者肝脏中酸性水解酶的总活性，对于β-半乳糖苷酶、α-半乳糖苷酶和芳基硫酸酯酶A而言有所降低；其他四种水解酶的总活性正常或升高。五种水解酶（β-葡萄糖醛酸酶、α-葡萄糖苷酶、β-半乳糖苷酶、N-乙酰-β-葡萄糖胺酶和α-半乳糖苷酶）的同工酶分布异常，即这些酶的等电点（通过等电聚焦法测定）比对照肝脏中的更偏酸性。除了同工酶异常外，不同种类的糖脂还贮积在肾脏、肝脏和大脑中。通过向正常肝脏匀浆中添加硫酸软骨素，可在体外重现同工酶异常，这表明黏多糖与水解酶分子之间发生了稳定结合。添加硫酸软骨素后，β-半乳糖苷酶的总活性受到抑制，而其他水解酶仅受到轻微影响或根本不受影响。
