Iwasaki Y, Tsuji A, Omura K, Suzuki Y
Department of Child Neurology, National Center Hospital for Mental, Nervous and Muscular Disorders, Tokyo.
J Biochem. 1989 Aug;106(2):331-5. doi: 10.1093/oxfordjournals.jbchem.a122853.
Lysosomal beta-mannosidase was purified almost 10,000-fold from human placenta. The final preparation showed several protein bands on polyacrylamide gel electrophoresis. Its molecular mass was estimated to be 110 kDa, the optimal pH was 4.5, the Km was 0.56 mM, and the isoelectric point was 4.7. The enzyme was found to bind completely to Con A-Sepharose, and the pI was not changed after neuraminidase treatment. These results indicate that the purified enzyme represents a lysosomal form which contains high mannose type oligosaccharide chains and only a few sialic acids, if any.
溶酶体β-甘露糖苷酶从人胎盘中纯化出来，纯化倍数近10000倍。最终制剂在聚丙烯酰胺凝胶电泳上显示出几条蛋白带。其分子量估计为110 kDa，最适pH为4.5，Km为0.56 mM，等电点为4.7。发现该酶能完全结合到伴刀豆球蛋白A-琼脂糖上，经神经氨酸酶处理后pI不变。这些结果表明，纯化后的酶代表一种溶酶体形式，其含有高甘露糖型寡糖链，且如果有唾液酸的话也只有少数。
