pAn alpha-D-galactosidase (EC 3.2.1.22) and a beta-D-mannanase (EC 3.2.1.78), which were secreted into the growth medium when Aspergillus tamarii was cultivated in the presence of galactomannan, were purified by a procedure including chromatography on hydroxyapatite and DEAE-cellulose columns. Each of these enzymes showed a single protein band, corresponding to their respective activities, on polyacrylamide-gel electrophoresis. Both enzymes were shown to be glycoproteins containing N-acetylglucosamine, mannose and galactose, with molar proportions of 1:6:1.5 for alpha-D-galactosidase and 1:13:8 for beta-D-mannanase. Mr values as determined by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate and by the electrophoretic method of Hedrick & Smith [(1968) Arch. Biochem. Biophys. 126, 155-164] were 56000 and 53000 respectively. The alpha-D-galactosidase differed markedly from the mycelial forms I and II studied in the preceding paper [Civas, Eberhard, Le Dizet & Petek (1984) Biochem. J. 219, 849-855] with regard to both its kinetic and structural properties./p
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机译：>通过在半乳甘露聚糖的存在下培养塔马里曲霉而分泌到生长培养基中的α-D-半乳糖苷酶（EC 3.2.1.22）和β-D-甘露聚糖酶（EC 3.2.1.78）通过该方法包括在羟基磷灰石和DEAE-纤维素柱上进行色谱分离。这些酶中的每一种在聚丙烯酰胺凝胶电泳上均显示出一条相应于其各自活性的蛋白带。两种酶均显示为含有N-乙酰氨基葡糖，甘露糖和半乳糖的糖蛋白，α-D-半乳糖苷酶的摩尔比例为1：6：1.5，β-D-甘露聚糖酶的摩尔比例为1：13：8。 Mr值是通过在十二烷基硫酸钠存在下的聚丙烯酰胺凝胶电泳和通过Hedrick＆amp; amp; amp;的电泳方法确定的。史密斯[（1968）拱。生化。生物物理学。 126、155-164]分别为56000和53000。 α-D-半乳糖苷酶与先前论文中研究的菌丝体形式I和II明显不同[Civas，Eberhard，Le Dizet＆amp; A. Petek（1984）生物化学。 J. 219，849-855]的动力学和结构特性。
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