Mathur R, Alvares K, Balasubramanian A S
Biochem Biophys Res Commun. 1984 Sep 28;123(3):1185-93. doi: 10.1016/s0006-291x(84)80258-2.
Lysosomal alpha-D-mannosidase of monkey brain existed in two forms. One form of mannosidase was bound to the Ricinus communis agglutinin120 (RCA1)-Sepharose and could be specifically eluted with lactose. The other form did not bind to the RCA1-Sepharose. Both forms of mannosidase could bind to a similar extent to the immobilized brain lysosomal receptor protein. Both the forms were purified to apparent homogeneity. Neutral sugar analysis by GLC showed the presence of glucose, mannose and galactose in the RCA1-Sepharose bindable mannosidase and glucose and mannose in the non-bindable mannosidase. Several other brain lysosomal hydrolases did not bind to the RCA1-Sepharose. The results suggested the existence of only high mannose oligosaccharides in the RCA1 non-bindable mannosidase and both high mannose and complex oligosaccharides in the bindable mannosidase.
猴脑溶酶体α-D-甘露糖苷酶存在两种形式。一种甘露糖苷酶与蓖麻凝集素120（RCA1）-琼脂糖结合，可用乳糖特异性洗脱。另一种形式不与RCA1-琼脂糖结合。两种形式的甘露糖苷酶与固定化脑溶酶体受体蛋白的结合程度相似。两种形式均被纯化至表观均一。通过气相色谱法进行的中性糖分析表明，RCA1-琼脂糖可结合的甘露糖苷酶中存在葡萄糖、甘露糖和半乳糖，而不可结合的甘露糖苷酶中存在葡萄糖和甘露糖。其他几种脑溶酶体水解酶不与RCA1-琼脂糖结合。结果表明，RCA1不可结合的甘露糖苷酶中仅存在高甘露糖型寡糖，而可结合的甘露糖苷酶中同时存在高甘露糖型和复杂型寡糖。
