Banno Y, Sasaki N, Miyawaki S, Kitagawa T, Nozawa Y
Biochem Med Metab Biol. 1986 Dec;36(3):322-32. doi: 10.1016/0885-4505(86)90143-x.
Various lysosomal acid hydrolases from tissues of Niemann-Pick mice, a mutant strain of C57BL/KsJ mice (spm/spm), were examined and compared to those from control mice. Activities of beta-hexosaminidase, beta-galactosidase, acid phosphatase, and cathepsin L were elevated in the liver and spleen of the affected mice, whereas no significant changes in beta-glucosidase and acid alpha-glucosidase were observed. Alpha-Mannosidase and neutral alpha-glucosidase activities were rather decreased in the affected mouse liver. The level of beta-hexosaminidase in the Niemann-Pick mice was raised sixfold in the liver and two- to threefold in the spleen and brain, whereas its total activity was decreased in the kidney. Sixty to ninety percent of total activity of lysosomal hydrolases was solubilized with 0.1% Triton X-100 in control mice, but most of the beta-hexosaminidase activity of the Niemann-Pick mice remained associated with the membrane fraction of liver lysosomes. The beta-hexosaminidase of the Niemann-Pick mice was appreciably stable when heated at 55 degrees C, while hydrolases of the affected mice and all of the enzymes tested in control mice were heat labile. The relative content of two beta-hexosaminidase fractions separated by DEAE-cellulose column chromatography was 8% for beta-hexosaminidase I and 92% for beta-hexosaminidase II in the case of the control mouse liver. The isozyme pattern of hexosaminidases in Niemann-Pick mice was similar to that of control enzymes. However, the beta-hexosaminidase II accumulated in Niemann-Pick mouse liver was different from that of the control in optimum pH, Km values and thermostability.
对C57BL/KsJ小鼠的突变品系（spm/spm）——尼曼-皮克小鼠组织中的多种溶酶体酸性水解酶进行了检测，并与对照小鼠的酶进行了比较。在患病小鼠的肝脏和脾脏中，β-己糖胺酶、β-半乳糖苷酶、酸性磷酸酶和组织蛋白酶L的活性升高，而β-葡萄糖苷酶和酸性α-葡萄糖苷酶未观察到显著变化。在患病小鼠肝脏中，α-甘露糖苷酶和中性α-葡萄糖苷酶的活性反而降低。尼曼-皮克小鼠肝脏中β-己糖胺酶的水平升高了6倍，脾脏和大脑中升高了2至3倍，而其在肾脏中的总活性降低。在对照小鼠中，溶酶体水解酶总活性的60%至90%可被0.1% Triton X-100溶解，但尼曼-皮克小鼠的大部分β-己糖胺酶活性仍与肝脏溶酶体的膜部分相关。当在55℃加热时，尼曼-皮克小鼠的β-己糖胺酶相当稳定，而患病小鼠的水解酶以及对照小鼠中测试的所有酶对热不稳定。通过DEAE-纤维素柱色谱分离的两种β-己糖胺酶组分的相对含量，在对照小鼠肝脏中，β-己糖胺酶I为8%，β-己糖胺酶II为92%。尼曼-皮克小鼠中己糖胺酶的同工酶模式与对照酶相似。然而，尼曼-皮克小鼠肝脏中积累的β-己糖胺酶II在最佳pH、Km值和热稳定性方面与对照不同。
