Muramatsu T, Koide N, Maeyama K
J Biochem. 1978 Feb;83(2):363-70. doi: 10.1093/oxfordjournals.jbchem.a131922.
The purification procedure for endo-beta-N-acetylglucosaminidase D was improved to yield an enzyme preparation which was homogeneous upon gel electrophoresis. The molecular weight of the enzyme as estimated by Sephadex G-200 column chromatography was 280,000, while SDS-gel electrophoresis after reduction with 2-mercaptoethanol gave a value of 150,000. The purified enzyme did not show any chitinase, hyaluronidase or lysozyme activity. In the presence of exoglycosidases removing peripheral sugars, the endoglycosidase acted on serum glycoproteins such as transferrin and fetuin. The enzyme also hydrolyzed an oligosaccharide, (Man)5(GlcNAc)2, indicating that the peptide portion of substrates does not have much effect on susceptibility to the enzyme.
β-N-乙酰氨基葡萄糖苷酶D的纯化程序得到了改进，从而获得了一种在凝胶电泳中呈均一状态的酶制剂。通过Sephadex G-200柱色谱法估计，该酶的分子量为280,000，而在用2-巯基乙醇还原后进行的SDS-凝胶电泳得出的值为150,000。纯化后的酶未表现出任何几丁质酶、透明质酸酶或溶菌酶活性。在存在去除外周糖的外切糖苷酶的情况下，内切糖苷酶作用于血清糖蛋白，如转铁蛋白和胎球蛋白。该酶还能水解一种寡糖（Man）5（GlcNAc）2，这表明底物的肽部分对酶的敏感性影响不大。
