Isolation and characterization of a blood group a substance degrading alpha n acetylgalactosaminidase from an acremonium sp
Isolation and characterization of a blood group a substance degrading alpha n acetylgalactosaminidase from an acremonium sp
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顶孢霉中降解 αn 乙酰半乳糖胺酶的血型的分离和表征
DOI：
10.1080/00021369.1989.10869270
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发表时间：
1989
期刊：
影响因子：
--
通讯作者：
T. Tochikura
中科院分区：
文献类型：
--
作者：
S. Kadowaki;Takeshi Ueda;Kenji Yamamoto;H. Kumagai;T. Tochikura
从土壤中分离的真菌在培养中产生α- n -乙酰半乳糖胺酶，该酶是主要的糖苷酶。根据各种分类特征，鉴定该真菌为Acremonium sp.。通过硫酸铵分离、DEAE-Sephadex A-50、羟磷灰石、Sephadex G-150和Concanavalin A-Sepharose 4B层析等步骤，从培养液中纯化出酶，达到电泳均匀性。经凝胶过滤和sds -聚丙烯酰胺凝胶电泳，酶的分子量分别为55,000和57,000，酶具有单体结构。该酶在pH 4.0 ~ 4.5时最具活性，在pH 6.0 ~ 7.5及低于40℃时较为稳定。/>-硝基苯基α- n -乙酰半乳糖胺的Michaelis常数为1.3 mm。该酶从用神经氨酸酶解解的牛颌下糖蛋白中释放出n -乙酰半乳糖胺。这种酶也可以…
A fungus isolated from soil was found to produce α-N-acetylgalactosaminidase in culture, this enzyme being the dominant glycosidase. The fungus was identified as an Acremonium sp., based on various taxonomical characteristics. The enzyme produced by the fungus was purified to electrophoretic homogeneity from the culture broth by procedures including ammonium sulfate fractionation, and chromatography on DEAE-Sephadex A-50, hydroxylapatite, Sephadex G-150 and Concanavalin A-Sepharose 4B. The molecular weight of the enzyme was estimated to be 55,000 and 57,000 by gel filtration and SDS-polyacrylamide gel electrophoresis, respectively, and the enzyme appeared to have a monomer structure. The enzyme was most active at pH 4.0 ~ 4.5, and was stable at pH 6.0 ~ 7.5 and below 40°C. The Michaelis constant for />-nitrophenyl α-N-acetylgalactosaminide was 1.3 mm. The enzyme liberated the N-acetylgalactosamine from the bovine submaxillary glycoprotein, which had been desialyzed with neuraminidase. The enzyme also libe...