Uchida Y, Tsukada Y, Sugimori T
J Biochem. 1977 Nov;82(5):1425-33. doi: 10.1093/oxfordjournals.jbchem.a131830.
Neuraminidase [sialidase, EC 3.2.1.18] was found to be widely distributed in bacteria belonging to Arthrobacter. Among these bacteria, Arthrobacter ureafaciens, A. oxydans, and A. aurescens produced relatively potent neuraminidase activities. For the production of this enzyme, not only colominic acid, a homopolymer of N-acetylneuraminic acid, but also N-acetylneuraminic acid, the reaction product of this enzyme, are effective as sources of carbon. An affinity adsorbent specific for neuraminidase was prepared by cross-linking colominic acid with soluble starch by means of epichlorohydrin. Neuraminidase from A. ureafaciens could be purified on this affinity column. The purified neuraminidase was shown to be free from protease, N-acetylneuraminic acid aldolase, phospholipase C, and glycosidases. Aminoff's assay procedure for sialic acid was modified to avoid the centrifugation step. The modified procedure gave a higher molecular extinction coefficient.
神经氨酸酶[唾液酸酶，EC 3.2.1.18]被发现广泛分布于节杆菌属细菌中。在这些细菌中，解脲节杆菌、氧化节杆菌和金色节杆菌产生相对较强的神经氨酸酶活性。对于这种酶的产生，不仅N-乙酰神经氨酸的同聚物共聚唾液酸是有效的碳源，而且该酶的反应产物N-乙酰神经氨酸也是有效的碳源。通过环氧氯丙烷将共聚唾液酸与可溶性淀粉交联，制备了一种对神经氨酸酶具有特异性的亲和吸附剂。解脲节杆菌的神经氨酸酶可以在该亲和柱上纯化。纯化后的神经氨酸酶被证明不含蛋白酶、N-乙酰神经氨酸醛缩酶、磷脂酶C和糖苷酶。对阿明诺夫唾液酸测定方法进行了改进，以避免离心步骤。改进后的方法给出了更高的分子消光系数。
