Wille W, Trenkner E
J Neurochem. 1981 Aug;37(2):443-6. doi: 10.1111/j.1471-4159.1981.tb00475.x.
The activity of particulate neuraminidase (sialidase, EC 3.2.1.18) in wild-type mice and the neurological mutant Staggerer was studied during development. Peak activity of this enzyme was observed at postnatal day 3 (P3) in three tissues of normal mice: cerebellum, cerebrum, and liver. In Staggerer, however, neuraminidase peak activity was observed at P27 in the cerebellum, whereas the activity was close to normal in Staggerer cerebrum and liver. Activities of the other glycosidases in Staggerer (alpha-glucosidase (pH 3.7), alpha-glucosidase (pH 6.0), N-acetyl-beta-hexosaminidase, beta-glucosidase, and beta-galactosidase) did not show significant variation compared with wild-type at P27 in any of the three tissues. This indicates that the late activity peak of particulate neuraminidase activity in the Staggerer cerebellum is neuraminidase-specific and not due to a general increase of lysosomal enzymes.
在发育过程中，对野生型小鼠和神经学突变体蹒跚鼠中颗粒神经氨酸酶（唾液酸酶，EC 3.2.1.18）的活性进行了研究。在正常小鼠的三种组织（小脑、大脑和肝脏）中，该酶的活性在出生后第3天（P3）达到峰值。然而，在蹒跚鼠中，神经氨酸酶的峰值活性在小脑的P27时才观察到，而在蹒跚鼠的大脑和肝脏中，该活性接近正常水平。与野生型相比，在P27时，蹒跚鼠的其他糖苷酶（α-葡萄糖苷酶（pH 3.7）、α-葡萄糖苷酶（pH 6.0）、N-乙酰-β-己糖胺酶、β-葡萄糖苷酶和β-半乳糖苷酶）在三种组织中的任何一种中均未显示出显著差异。这表明，蹒跚鼠小脑中颗粒神经氨酸酶活性的晚期峰值是神经氨酸酶特异性的，并非由于溶酶体酶的普遍增加所致。
