黑曲霉中诱导产生的糖苷酶。菌丝体α-D-半乳糖苷酶。
Glycosidases induced in Aspergillus tamarii. Mycelial alpha-D-galactosidases.
作者信息
Civas A, Eberhard R, Le Dizet P, Petek F
出版信息
Biochem J. 1984 May 1;219(3):849-55. doi: 10.1042/bj2190849.
Two alpha-D-galactosidases (alpha-D-galactoside galactohydrolase, EC 3.2.1.22) produced by Aspergillus tamarii were purified from the mycelial extract by a procedure including chromatography on hydroxyapatite, DEAE-cellulose and ECTEOLA-cellulose. Each of these enzymes showed a single protein band corresponding to the alpha-D-galactosidase activity when examined by polyacrylamide-gel electrophoresis. They catalysed the hydrolysis of o-nitrophenyl alpha-D-galactoside, melibiose, raffinose and stachyose, but did not attack the galactomannans. Their Mr values were respectively 265000 +/- 5000 and 254000 +/- 5000 by the method of Hedrick & Smith [(1968) Arch. Biochem. Biophys. 126, 155-164]. Polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate in each case showed a single protein band, with Mr 88000 and 77500 respectively. The purified enzymes contained carbohydrate, consisting of N-acetylglucosamine, mannose, glucose and galactose in the estimated molar proportions of 1:9:5:8 in alpha-galactosidase I.
由塔玛曲霉产生的两种α-D-半乳糖苷酶（α-D-半乳糖苷半乳糖水解酶，EC 3.2.1.22）通过包括在羟基磷灰石、DEAE-纤维素和ECTEOLA-纤维素上进行色谱分离的程序从菌丝体提取物中纯化得到。当通过聚丙烯酰胺凝胶电泳检测时，每种酶都显示出一条与α-D-半乳糖苷酶活性相对应的单一蛋白带。它们催化邻硝基苯基α-D-半乳糖苷、蜜二糖、棉子糖和水苏糖的水解，但不作用于半乳甘露聚糖。根据赫德里克和史密斯的方法[（1968年）《生物化学与生物物理学文献》126，155 - 164]，它们的相对分子质量分别为265000±5000和254000±5000。在十二烷基硫酸钠存在下进行的聚丙烯酰胺凝胶电泳在每种情况下均显示出一条单一蛋白带，相对分子质量分别为88000和77500。纯化后的酶含有碳水化合物，在α-半乳糖苷酶I中，由N-乙酰葡糖胺、甘露糖、葡萄糖和半乳糖组成，估计摩尔比例为1:9:5:8。
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