Leung K C, Fung K P, Yu C C, Choy Y M, Lee C Y
Clin Chim Acta. 1977 Jan 3;74(1):43-9. doi: 10.1016/0009-8981(77)90386-2.
The N-acetyl-beta-glucosaminidase activity in hydatidiform mole is two-fold higher than that in full-term placenta. Qualitatively, the enzymes from the two tissues are similar with respect to KM values and pH optima. Both enzymes also contain a new isoenzyme form detectable by polyacrylamide gel electrophoresis. However, the molar enzyme is more susceptible to heat denaturation, presumably due to the presence of a higher level of the heat-labile isoenzyme form A in this tissue. Data are also presented incicating that the placenta is not the source of the N-acetyl-beta-glucosaminidase activity in maternal serum.
葡萄胎中N-乙酰-β-葡萄糖苷酶的活性比足月胎盘高两倍。从性质上讲,这两种组织中的酶在米氏常数(KM值)和最适pH方面相似。两种酶都含有一种可通过聚丙烯酰胺凝胶电泳检测到的新同工酶形式。然而,葡萄胎中的酶更易受热变性,推测是由于该组织中存在较高水平的热不稳定同工酶形式A。还提供了数据表明胎盘不是母体血清中N-乙酰-β-葡萄糖苷酶活性的来源。