Chester M A, Lundblad A, Masson P K
Biochim Biophys Acta. 1975 Jun 24;391(2):341-8. doi: 10.1016/0005-2744(75)90258-2.
The tissue distribution and some properties of human alpha-mannosidase (alpha-D-mannoside mannohydrolase EC 3.2.1.24) have been studied. The acidic forms of the enzyme were fairly stable, whereas the neutral forms easily lost enzymic activity. The acidic forms were sensitive to neuraminidase but the neutral forms were unaffected. The experiments indicate that the acidic components are closely related to each other, differing only in sialic acid content and possibly conformation. The neutral forms of the enzyme are probably quite different from the acidic forms both in structure and cellular function.
已对人α-甘露糖苷酶（α-D-甘露糖苷甘露水解酶，EC 3.2.1.24）的组织分布及某些特性进行了研究。该酶的酸性形式相当稳定，而中性形式则容易丧失酶活性。酸性形式对神经氨酸酶敏感，但中性形式不受影响。实验表明，酸性组分彼此密切相关，仅在唾液酸含量和可能的构象上有所不同。该酶的中性形式在结构和细胞功能上可能与酸性形式有很大差异。
