Civas A, Eberhard R, Le Dizet P, Petek F
Biochem J. 1984 May 1;219(3):857-63. doi: 10.1042/bj2190857.
An 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.
当黑曲霉在半乳甘露聚糖存在的条件下培养时，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），通过包括在羟基磷灰石和DEAE-纤维素柱上进行层析的方法进行纯化。在聚丙烯酰胺凝胶电泳上，这些酶各自都显示出一条对应其各自活性的单一蛋白带。两种酶均被证明是含有N-乙酰葡糖胺、甘露糖和半乳糖的糖蛋白，α-D-半乳糖苷酶中三者的摩尔比例为1:6:1.5，β-D-甘露聚糖酶中三者的摩尔比例为l:13:8。在十二烷基硫酸钠存在下通过聚丙烯酰胺凝胶电泳以及采用赫德里克和史密斯的电泳方法[（1968年）《生物化学与生物物理学文献》126, 155 - 164]测定的相对分子质量分别为56000和53000。α-D-半乳糖苷酶在动力学和结构性质方面与前文[西瓦斯、埃伯哈德、勒迪泽和彼得克（1984年）《生物化学杂志》219, 849 - 855]中研究的菌丝体I型和II型明显不同。
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